Source 1primary paper2023Research Square (Research Square)
Toolkit/GFP-PHR-caspase8/Flag-CIB1N-caspase8
GFP-PHR-caspase8/Flag-CIB1N-caspase8
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
GFP-PHR-caspase8/Flag-CIB1N-caspase8 is a blue light-responsive two-component optogenetic caspase-8 system composed of GFP-PHR-caspase8 and Flag-CIB1N-caspase8 fusion proteins. Under blue light, the two components interact more strongly and undergo light-dependent cleavage, consistent with inducible caspase-8 activation.
Usefulness & Problems
Why this is useful
This system provides optical control over caspase-8-associated cell death signaling using a genetically encoded two-component switch. Reported use cases include stronger apoptosis induction in the Opto-Casp8-V2 configuration and regulation of inflammasome activation and pyroptosis under conditions where apoptosis and necroptosis are compromised.
Source:
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
Source:
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
Problem solved
It addresses the need for temporally controlled activation of caspase-8-dependent death pathways with light rather than constitutive or chemically induced activation. The available evidence specifically supports blue light-dependent interaction and cleavage of the fused caspase-8 components.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
caspase activationlight-induced protein-protein interactionPhotocleavageproteolytic self-cleavageTechniques
Functional AssayTarget processes
recombinationInput: Light
Implementation Constraints
The construct architecture consists of GFP-PHR fused to caspase-8 and Flag-CIB1N fused to caspase-8, indicating a domain-fusion, two-component design. Blue light is the activating input, and co-immunoprecipitation was used to assess light-enhanced interaction; no additional practical details such as expression system, chromophore requirements, or delivery method are specified in the supplied evidence.
The evidence provided is limited to a single 2023 Research Square source and a small number of reported observations. Quantitative performance metrics, illumination parameters, cell-type scope, reversibility, background activity in the dark, and independent replication are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Linemechanistic demo
Inferred from claim c2 during normalization. Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation. Derived from claim c2. Quoted text: After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
successMammalian Cell Lineapplication demo
co-immunoprecipitation
Inferred from claim c3 during normalization. GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays. Derived from claim c3. Quoted text: The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
successMammalian Cell Lineapplication demo
Inferred from claim c7 during normalization. Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised. Derived from claim c7. Quoted text: Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
Supporting Sources
Ranked Claims
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced nuclear shrinkage, apoptotic body formation, and cell death.
Both Opto-Casp8-V1 and Opto-Casp8-V2 induced the shrinkage of numerous nuclei, leading to the formation of apoptotic bodies and ultimately promoting cell death.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug gfp-phr-caspase8-flag-cib1n-caspase8
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
conditional functionsupports
Under blue light control, the tool regulates inflammasome activation and induces pyroptosis when apoptosis and necroptosis mechanisms are compromised.
Additionally, through blue light control, it regulates the activation of the inflammasome and induction of pyroptosis in cases where apoptosis and necroptosis mechanisms are compromised.
Source:
interaction or cleavagesupports
GFP-PHR-caspase8 and Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and showed stronger interaction in co-immunoprecipitation assays.
The proteins GFP-PHR-caspase8/Flag-CIB1N-caspase8 were cleaved in a blue light-dependent manner and interacted more strongly in co-immunoprecipitation assays.
Source:
mechanistic effectsupports
Blue light exposure decreased precursor PHR-Caspase8 abundance and increased activated caspase-8 (P18) and caspase-3 accumulation.
After exposure to blue light, the abundance of the precursor protein PHR-Caspase8 decreased, while the activated forms of caspase8 (P18) and caspase3 accumulated.
Source:
tool functionsupports
The optogenetic tool enables precise modulation of caspase-8 activity to induce cellular apoptosis.
Our optogenetic tool enables precise modulation of Caspase-8 activity, inducing cellular apoptosis.
Source:
tool functionsupports
The study developed an optogenetic approach that rapidly modulates caspase-8 activation in response to blue light.
In this study, we developed an optogenetic approach to rapidly modulate the activation of caspase-8 in response to blue light.
Source:
Comparisons
Source-backed strengths
The source reports blue light-dependent cleavage of both GFP-PHR-caspase8 and Flag-CIB1N-caspase8 together with stronger interaction in co-immunoprecipitation assays. Comparative evidence further states that Opto-Casp8-V2 showed more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light and promoted apoptosis more strongly.
Source:
Opto-Casp8-V2 exhibited significantly more efficient self-cleavage and consumption than Opto-Casp8-V1 under blue light, and was found to promote cell apoptosis more strongly.
Ranked Citations
- 1.