Source 1primary paper2021PLoS Genetics
Toolkit/photo-N-degron
photo-N-degron
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The photo-N-degron is a peptide tag for optogenetic control of protein function in vivo through light-mediated protein degradation. It was reported to direct light-dependent degradation in Saccharomyces cerevisiae and Drosophila melanogaster, including light-dependent loss of Cactus function in developing Drosophila embryos.
Usefulness & Problems
Why this is useful
This tool enables temporal control of protein function by coupling illumination to targeted protein destabilization in vivo. The reported activity in both yeast and Drosophila indicates utility for perturbing developmental and cellular processes with light.
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
The photo-N-degron addresses the problem of disrupting protein function with fine temporal control in living systems. The cited study specifically used it to induce light-dependent loss of Cactus function in Drosophila embryos.
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.
Mechanisms
Conformational UncagingDegradationlight-dependent conformational uncagingn-end rule-mediated degradationprotein degradationTechniques
No technique tags yet.
Target processes
degradationInput: Light
Implementation Constraints
The tool is described as a peptide tag, indicating implementation by fusion to a protein of interest. The supplied evidence supports use in Saccharomyces cerevisiae and Drosophila melanogaster, but does not provide construct architecture, cofactor requirements, or delivery details.
The supplied evidence comes from a single 2021 study and is limited to in vivo use in yeast and Drosophila. No quantitative performance metrics, illumination wavelengths, degradation kinetics, or generality across many target proteins are provided in the supplied evidence.
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 source5 linked approval claimsfirst-pass slug photo-n-degron
the photo-N-degron, a peptide tag that can be used in optogenetic studies of protein function in vivo
Source:
applicationsupports
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.
Source:
comparative effectivenesssupports
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.
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:
mechanismsupports
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.
Source:
tool developmentsupports
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.
Source:
Comparisons
Source-backed strengths
The source literature reports light-mediated degradation with fine temporal control in Saccharomyces cerevisiae and Drosophila melanogaster. In developing Drosophila embryos, the photo-N-degron was effective in eliciting light-dependent loss of Cactus function as assessed by dorsal-ventral patterning phenotypes, and the related B-LID domain was also reported as effective in this context.
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.