Source 1primary paper2021PLoS Genetics
Toolkit/blue light-inducible degradation (B-LID) domain
blue light-inducible degradation (B-LID) domain
Also known as: B-LID
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The blue light-inducible degradation (B-LID) domain is a light-activated degron used to trigger loss of a fused protein in vivo. Available evidence indicates that it must be fused to the carboxy terminus of the target protein and can elicit light-dependent loss of Cactus function in developing Drosophila embryos.
Usefulness & Problems
Why this is useful
B-LID is useful for inducing protein loss with light, enabling temporal control of protein function in vivo. The supplied evidence specifically supports its use for light-dependent disruption of Cactus function during Drosophila embryogenesis.
Source:
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
Source:
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
Problem solved
B-LID helps solve the problem of controlling protein degradation with external light input rather than constitutive genetic perturbation. The evidence supports this as a way to achieve temporally controlled loss of target protein function in living systems.
Source:
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
Source:
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
degradationInput: Light
Implementation Constraints
Available evidence indicates that B-LID must be fused to the C terminus of the target protein. No additional implementation details such as cofactor requirements, expression system constraints, or illumination parameters are provided in the supplied evidence.
The supplied evidence provides only limited mechanistic and performance detail for B-LID, with no quantitative degradation kinetics, dynamic range, or wavelength specification. It also indicates a construct constraint, namely that the domain must be placed at the carboxy terminus of the targeted protein.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
The photo-N-degron can direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
We demonstrate that the photo-N-degron can be used to direct light-mediated degradation of proteins in Saccharomyces cerevisiae and Drosophila melanogaster with fine temporal control.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
In Drosophila embryos, the photo-N-degron is effective in eliciting light-dependent loss of Cactus function as determined by dorsal-ventral patterning phenotypes.
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
The photosensitive degron (psd) has little effect on Cactus-dependent phenotypes in response to illumination of developing embryos.
another previously described photosensitive degron (psd), which also must be located at the carboxy terminus of associated proteins, has little effect on Cactus-dependent phenotypes in response to illumination of developing embryos.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
When fused to amino termini of proteins, the photo-N-degron undergoes a blue light-dependent conformational change that exposes a signal for N-recognins mediating N-end rule proteasomal degradation.
The photo-N-degron can be expressed as a genetic fusion to the amino termini of other proteins, where it undergoes a blue light-dependent conformational change that exposes a signal for the class of ubiquitin ligases, the N-recognins, which mediate the N-end rule mechanism of proteasomal degradation.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
The photo-N-degron is a peptide tag developed for optogenetic studies of protein function in vivo.
Here we describe the development and characterization of the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug blue-light-inducible-degradation-b-lid-domain
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins
Source:
comparative effectivenesssupports
The B-LID domain is effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos.
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
Source:
design constraintsupports
The photo-N-degron functions as an N-terminal fusion and the B-LID domain functions as a C-terminal fusion to support light-dependent degradation in vivo.
importantly demonstrate that N- and C-terminal fusions to the photo-N-degron and the B-LID domain, respectively, support light-dependent degradation in vivo.
Source:
Comparisons
Source-backed strengths
The domain is explicitly described as a light-activated degron and was reported to be effective in eliciting light-dependent loss of Cactus function in developing Drosophila embryos. The same study also presents a broader context of light-mediated protein disruption in Saccharomyces cerevisiae and Drosophila melanogaster, although the organism-specific breadth for B-LID itself is limited in the supplied evidence.
Source:
We find that like the photo-N-degron, the blue light-inducible degradation (B-LID) domain ... is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
Source:
the blue light-inducible degradation (B-LID) domain, a light-activated degron that must be placed at the carboxy terminus of targeted proteins, is also effective in eliciting light-dependent loss of Cactus function, as determined by embryonic dorsal-ventral patterning phenotypes.
Source:
another previously described photosensitive degron (psd), which also must be located at the carboxy terminus of associated proteins, has little effect on Cactus-dependent phenotypes in response to illumination of developing embryos.
Ranked Citations
- 1.