PhyB/PIF

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Clinical application of optogenetic gene regulation is limited by unanswered questions including exogenous chromophore use and gentle but effective transfection methods for in vivo applications.

Among the many unanswered questions concerning the application of optogenetics, we discuss items such as the use of exogenous chromophores and their effects on the biology of the cells and methods for a gentle, but effective gene transfection method for optogenetic tools for in vivo applications.

Phytochromes have an intrinsic advantage over other photoreceptor classes because their bidirectional dual-wavelength control enables instant ON and OFF regulation.

This compilation illustrates the intrinsic advantages of phytochromes compared to other photoreceptor classes, e.g., their bidirectional dual-wavelength control enabling instant ON and OFF regulation.

Phytochrome-based optogenetic tools are implemented across bacteria, yeast, plants, and animals to control diverse biological activities.

Phytochrome-based optogenetic tools are currently implemented in bacteria, yeast, plants, and animals to achieve light control of a wide range of biological activities.

The review describes engineering of phytochromes to improve them as photoswitches and surveys their use in optogenetic applications.

Based on this knowledge, we then describe the engineering of phytochromes to further improve these chromoproteins as photoswitches and review their employment in an ever-growing number of different optogenetic applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

The long-wavelength absorption and fluorescence of phytochromes within the transparent window make them attractive for applications requiring deep tissue penetration or combination with blue and UV light-sensing photoreceptors.

In particular, the long wavelength range of absorption and fluorescence within the "transparent window" makes phytochromes attractive for complex applications requiring deep tissue penetration or dual-wavelength control in combination with blue and UV light-sensing photoreceptors.

The PhyB-PIF light-inducible dimerization system controls both association and dissociation by light on the second time scale.

has a unique property of controlling both association and dissociation by light on the second time scale

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Drug inducible lentiviral and transposon vectors carrying PhyB-PIF and synPCB enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Concatenating the PCB synthesis genes with P2A peptide cDNAs for polycistronic expression resulted in an approximately 4-fold increase in PCB synthesis compared with the previous version.

these genes were concatenated with P2A peptide cDNAs for polycistronic expression, resulting in an approximately 4-fold increase in PCB synthesis compared with the previous version

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

The improved synPCB design increased PCB synthesis by approximately 4-fold compared with the previous version.

resulting in an approximately 4-fold increase in PCB synthesis compared with the previous version

The improved synPCB design increased PCB synthesis by approximately 4-fold compared with the previous version.

resulting in an approximately 4-fold increase in PCB synthesis compared with the previous version

The improved synPCB design increased PCB synthesis by approximately 4-fold compared with the previous version.

resulting in an approximately 4-fold increase in PCB synthesis compared with the previous version

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

Depletion of biliverdin reductase A increases intracellular phycocyanobilin concentration.

An even higher intracellular PCB concentration was achieved by the depletion of biliverdin reductase A, which degrades PCB.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

An expression vector coexpressing HO1, PcyA, ferredoxin, and ferredoxin-NADP+ reductase enables efficient synthesis of phycocyanobilin in mammalian cell mitochondria.

Here, we report an expression vector that coexpresses HO1 and PcyA with Ferredoxin and Ferredoxin-NADP+ reductase for the efficient synthesis of PCB in the mitochondria of mammalian cells.

The paper demonstrates in vivo manipulation of the polarity protein Pard3 using the PHYB/PIF optogenetic localization system.

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

PCB is required for use of the PHYB/PIF system in vertebrate embryos because vertebrate cells do not naturally produce the phytochrome chromophore.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PIF4 levels and regulates light-responsive gene expression.

Manipulating PCH1 alters PHYTOCHROME INTERACTING FACTOR 4 levels and regulates light-responsive gene expression.

The study describes optimization of the Arabidopsis PHYB/PIF6 red/far-red optogenetic heterodimerization system for live zebrafish embryos to enable rapid, reversible subcellular protein recruitment.

Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

PIF4 and PIF5 regulate elongation growth by directly controlling expression of genes encoding auxin biosynthesis and auxin signaling components.

our study suggests that PIF4 and PIF5 regulate elongation growth by controlling directly the expression of genes that code for auxin biosynthesis and auxin signaling components

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Shade avoidance in dense vegetation is triggered at least partially by reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

Degradation of PIF4 and PIF5 is preceded by phosphorylation, requires the APB domain, and is sensitive to proteasome inhibitors, suggesting degradation upon interaction with light-activated phyB.

Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including early flowering, are similar to those of phyB mutants.

The developmental morphologies of PIL6-ox, including the phenotype of early flowering, were also similar to those of phyB mutants.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with phytochrome species is transient.

Rapid light-induced degradation of PIF3 indicates that interaction of PIF3 with these phytochrome species is transient.

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

Light-induced PIF3 degradation is controlled by the concerted action of phyA, phyB, and phyD photoreceptors.

This process is controlled by the concerted action of the R/FR absorbing phyA, phyB, and phyD photoreceptors

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

PIL6-ox plants are hyposensitive to red light.

transgenic plants overexpressing PIL6 (PIL6-ox) are hyposensitive to red light under the same conditions

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The pil6-1 loss-of-function mutant is hypersensitive to red light in seedling de-etiolation.

the loss-of-function mutant (pil6-1) showed a remarkable phenotype in that it is hypersensitive to red light in seedling de-etiolation

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hypersensitive phenotype of pil6-1 is similar to that of transgenic lines overexpressing TOC1/APRR1.

This phenotype was similar to that observed for transgenic lines overexpressing TOC1 (or APRR1).

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

The red-light hyposensitive phenotype of PIL6-ox is very similar to that of phyB mutants.

This phenotype was very similar to that observed for phyB mutants.

Applications of phytochrome-based tools include regulation of gene expression, protein transport into cell organelles, and recruitment of tagged proteins to membranes and other cellular compartments.

These cover the regulation of gene expression, protein transport into cell organelles, and the recruitment of phytochrome- or PIF-tagged proteins to membranes and other cellular compartments.

Source: The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters

Optogenetic gene regulation may enable spatially and temporally regulated gene and protein expression for cell therapeutic approaches.

Here optogenetic gene regulation might offer an excellent method for spatially and timely regulated gene and protein expression in cell therapeutic approaches.

Source: Clinical applicability of optogenetic gene regulation

Most phytochrome optogenetic applications described in the review rely on the light-controlled interaction between PhyB and PIFs or on C-terminal light-regulated enzymatic domains from bacterial and algal phytochromes.

Most applications rely on the light-controlled complex formation between the plant photoreceptor PhyB and phytochrome-interacting factors (PIFs) or C-terminal light-regulated domains with enzymatic functions present in many bacterial and algal phytochromes.

Source: The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters

This review focuses on optogenetic control of gene expression in mammalian cells as models relevant to clinical applications.

This review will be confined to the optogenetic control of gene expression in mammalian cells as suitable models for clinical applications.

Source: Clinical applicability of optogenetic gene regulation

Incorporation of PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors enabled doxycycline-inducible PCB synthesis and PhyB-PIF light-inducible dimerization system expression or function.

we incorporated PhyB-PIF and synPCB into drug inducible lentiviral and transposon vectors, which enabled us to induce PCB synthesis and PhyB-PIF LID system by doxycycline treatment

Source: Improvement of phycocyanobilin synthesis for genetically encoded phytochrome-based optogenetics

The PhyB-PIF red/far-red responsive light-inducible dimerization system requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin.

PhyB requires a linear tetrapyrrole chromophore such as phytochromobilin or phycocyanobilin (PCB)

Source: Improvement of phycocyanobilin synthesis for genetically encoded phytochrome-based optogenetics

The authors successfully established a stable cell line containing a genetically encoded PhyB-PIF light-inducible dimerization system.

successfully established a stable cell line containing a genetically encoded PhyB-PIF LID system

Source: Improvement of phycocyanobilin synthesis for genetically encoded phytochrome-based optogenetics

The PCB synthesis system together with the PhyB-PIF system enables optogenetic regulation of intracellular signaling without external chromophore supply.

The PCB synthesis and PhyB-PIF systems allowed us to optogenetically regulate intracellular signaling without any external supply of chromophores.

Source: Efficient synthesis of phycocyanobilin in mammalian cells for optogenetic control of cell signaling

This work provides a practical method for a fully genetically encoded PhyB-PIF system.

Thus, we have provided a practical method for developing a fully genetically encoded PhyB-PIF system, which paves the way for its application to a living animal.

Source: Efficient synthesis of phycocyanobilin in mammalian cells for optogenetic control of cell signaling

The paper demonstrates in vivo manipulation of the polarity protein Pard3 using the PHYB/PIF optogenetic localization system.

Source: Reversible Optogenetic Control of Subcellular Protein Localization in a Live Vertebrate Embryo

PCH1 binds phytochrome B in a red light-dependent manner.

PCH1 peaks at dusk, binds phytochrome B (phyB) in a red light-dependent manner

Source: PCH1 integrates circadian and light-signaling pathways to control photoperiod-responsive growth in Arabidopsis

PCB is required for use of the PHYB/PIF system in vertebrate embryos because vertebrate cells do not naturally produce the phytochrome chromophore.

Source: Reversible Optogenetic Control of Subcellular Protein Localization in a Live Vertebrate Embryo

PCH1 co-localizes with phytochrome B into photobodies.

and co-localizes with phyB into photobodies.

Source: PCH1 integrates circadian and light-signaling pathways to control photoperiod-responsive growth in Arabidopsis

PCH1 regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB signaling.

Thus, PCH1 is a new factor that regulates photoperiod-responsive growth by integrating the clock with light perception pathways through modulating daily phyB-signaling.

Source: PCH1 integrates circadian and light-signaling pathways to control photoperiod-responsive growth in Arabidopsis

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies and maintain an active phyB pool after light exposure.

PCH1 is necessary and sufficient to promote the biogenesis of large photobodies to maintain an active phyB pool after light exposure

Source: PCH1 integrates circadian and light-signaling pathways to control photoperiod-responsive growth in Arabidopsis

The study describes optimization of the Arabidopsis PHYB/PIF6 red/far-red optogenetic heterodimerization system for live zebrafish embryos to enable rapid, reversible subcellular protein recruitment.

Source: Reversible Optogenetic Control of Subcellular Protein Localization in a Live Vertebrate Embryo

Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.

Source: Optogenetic control of signaling in mammalian cells

Phytochrome B is the major light sensor mediating the adaptive shade-avoidance response.

The phytochrome B (phyB) photoreceptor is the major light sensor to mediate this adaptive response.

Source: Phytochrome interacting factors 4 and 5 control seedling growth in changing light conditions by directly controlling auxin signaling

Phytochrome B directly controls the protein abundance of PIF4 and PIF5 as part of shade-avoidance syndrome control.

Control of the SAS occurs in part with phyB, which controls protein abundance of phytochrome-interacting factors 4 and 5 (PIF4 and PIF5) directly.

Source: Phytochrome interacting factors 4 and 5 control seedling growth in changing light conditions by directly controlling auxin signaling

The constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Consistent with this idea, the constitutive shade-avoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

Source: Phytochrome‐mediated inhibition of shade avoidance involves degradation of growth‐promoting bHLH transcription factors