Source 1primary paper2022The FASEB Journal
Toolkit/optoPAK1
optoPAK1
Also known as: optogenetic analog of PAK1
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
optoPAK1 is a genetically encoded, light-responsive optogenetic analog of p21-activated kinase 1 (PAK1) engineered for photoinduced recruitment to specified intracellular sites. It was designed as a constitutively active PAK1 variant that functions independently of endogenous biochemical regulation while maintaining minimal dark-state activity.
Usefulness & Problems
Why this is useful
optoPAK1 is useful for light-controlled spatial regulation of PAK1 localization inside cells. Its design aims to decouple PAK1 activity from endogenous upstream regulation while enabling illumination-dependent targeting to defined subcellular locations.
Problem solved
optoPAK1 addresses the problem of controlling PAK1 signaling with subcellular precision using light rather than native biochemical inputs. The reported design specifically seeks to provide constitutive PAK1 activity with low activity in the dark state and light-triggered intracellular relocalization.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Computational DesignTarget processes
recombinationInput: Light
Implementation Constraints
The available evidence indicates that optoPAK1 is a genetically expressed construct and that its function involves illumination-dependent migration to specified intracellular sites. The current summary additionally states use of the iLid light-induced dimerization system for subcellular recruitment, but the provided source excerpts do not supply construct architecture, cofactors, expression conditions, or targeting-module details.
The supplied evidence does not report quantitative performance metrics, illumination wavelengths, kinetics, dynamic range, or validation across multiple biological contexts. Independent replication is not evident from the provided source set.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Approval Evidence
1 source5 linked approval claimsfirst-pass slug optopak1
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
Source:
design propertysupports
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.
Source:
engineering resultsupports
The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
Source:
localization controlsupports
Upon illumination, optoPAK1 migrates to specified intracellular sites.
upon illumination, optoPAK1 migrates to specified intracellular sites
Source:
mechanism of controlsupports
The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.
We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.
Source:
reporter responsesupports
Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.
preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion
Source:
Comparisons
Source-backed strengths
The reported strengths are that optoPAK1 is genetically encoded, light responsive, and capable of migrating to specified intracellular sites upon illumination. It was also designed to operate independently of endogenous biochemical regulation in a constitutively active manner with minimal dark-state activity.
Source:
We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)
Ranked Citations
- 1.