Source 1primary paper2015Nature Communications
Toolkit/Magnets
Magnets
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Magnets are engineered pairs of distinct light-responsive protein modules derived from the Neurospora crassa photoreceptor Vivid. They act as a multi-component optogenetic switch by converting a native Vivid homodimerization interface into complementary light-dependent heterodimers for protein interaction and recruitment in subcellular volumes.
Usefulness & Problems
Why this is useful
Magnets enable optogenetic control of protein recruitment and interaction with high spatial subcellular confinement. Reported applications include rapid and reversible recruitment of proteins to subcellular organelles, induction of organelle contacts, and reconstitution of OSBP-VAP endoplasmic reticulum-Golgi tethering.
Source:
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
Source:
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Source:
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
Source:
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Problem solved
This tool addresses the need for light-gated, spatially confined control of protein-protein association inside cells. The optimized eMags variant specifically addresses earlier practical constraints by eliminating the need for concatemerization and 28°C preincubation for functionality.
Source:
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
Source:
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
Heterodimerizationlight-dependent heterodimerizationsimultaneous dual-component photoactivationTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
Magnets are implemented as a two-component system composed of distinct Vivid-derived photoswitch modules engineered to heterodimerize upon illumination. Earlier versions required concatemerization and 28°C cell preincubation, whereas optimized eMags were reported to function without those requirements; the provided evidence does not specify construct architecture beyond derivation from Vivid and use for subcellular recruitment.
The literature indicates that Magnets originally required concatemerization for efficient responses and cell preincubation at 28°C to be functional. The supplied evidence does not provide additional quantitative performance metrics, spectral details, or validation outside the cited subcellular optogenetic applications.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2018Proceedings of the National Academy of Sciences
Source 3primary paper2020
Ranked Claims
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
eMags can be used to rapidly and reversibly recruit proteins to subcellular organelles, induce organelle contacts, and reconstitute OSBP-VAP ER-Golgi tethering.
We validated these “enhanced” Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
The optimized Magnets pair eMags requires neither concatemerization nor low temperature preincubation.
Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
preincubation temperature 28 °C
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags are presented as an effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
switch-off kinetics tuning range four orders of magnitude
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
Approval Evidence
3 sources12 linked approval claimsfirst-pass slug magnets
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Source:
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Source:
pairs of distinct photoswitches named Magnets
Source:
limitationsupports
Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
However, Magnets require concatemerization for efficient responses and cell preincubation at 28°C to be functional.
Source:
mechanism propertysupports
Both Magnets components require simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength.
Source:
tool origin or designsupports
Magnets are engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
Magnets are small modules engineered from the Neurospora crassa photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers.
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comparative performancesupports
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
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design rulesupports
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
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determinant of spatial confinementsupports
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
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tradeoffsupports
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
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application utilitysupports
Magnets can be used as optogenetic tools to manipulate molecular processes in biological systems.
We demonstrate the utility of Magnets as powerful tools that can optogenetically manipulate molecular processes in biological systems.
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comparative performancesupports
Some Magnets variants have substantially faster kinetics than other conventional dimerization-based blue spectrum photoswitches.
developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
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engineering resultsupports
The authors engineered the fungal photoreceptor Vivid to develop pairs of distinct photoswitches called Magnets.
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
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kinetic tuningsupports
The switch-off kinetics of Magnets were tuned across four orders of magnitude.
we tuned the switch-off kinetics by four orders of magnitude
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mechanism propertysupports
Magnets were engineered to recognize each other through electrostatic interactions, preventing homodimerization and enhancing light-induced heterodimerization.
These new photoswitches were engineered to recognize each other based on the electrostatic interactions, thus preventing homodimerization and enhancing light-induced heterodimerization.
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Comparisons
Source-backed strengths
Magnets were engineered as complementary heterodimeric photoswitches from the small fungal photoreceptor Vivid, and they have been quantitatively compared with Cry2/CIB1 and iLID for light-dependent dimer occurrence in small subcellular volumes. The optimized eMags pair was reported to support rapid and reversible subcellular recruitment and organelle-contact manipulation without requiring concatemerization or low-temperature preincubation.
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Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation.
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Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
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developed several variants, including those with substantially faster kinetics than any of the other conventional dimerization-based blue spectrum photoswitches
Source:
we completed a multi-directional engineering of the fungal photoreceptor Vivid to develop pairs of distinct photoswitches named Magnets
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