Source 1primary paper2019Carolina Digital Repository (University of North Carolina at Chapel Hill)
Toolkit/optogenetic protein kinase A
optogenetic protein kinase A
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Optogenetic protein kinase A is a light-controlled multi-component switch for probing localized protein kinase A signaling. It uses the Cry2-Cib photodimerizing pair to translocate a low-constitutive-activity protein kinase A catalytic subunit to a Cib-defined subcellular site, where kinase activity is restored.
Usefulness & Problems
Why this is useful
This tool is useful for investigating localized functions of protein kinase A with optical control over subcellular recruitment. The available evidence indicates that it was developed specifically to study spatial aspects of kinase signaling rather than bulk pathway activation alone.
Source:
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Source:
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
Problem solved
It addresses the problem of controlling protein kinase A activity at defined subcellular regions to dissect localized signaling functions. The cited work frames this as part of cellular optogenetics for spatiotemporal control of kinase signaling.
Source:
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
Problem links
Need conditional control of signaling activity
DerivedOptogenetic protein kinase A is a light-controlled, multi-component switch built around the Cry2-Cib photodimerizing pair to investigate localized protein kinase A function. Upon light stimulation, a low-constitutive-activity protein kinase A catalytic subunit is translocated to a Cib-defined subcellular site, where kinase activity is restored.
Need precise spatiotemporal control with light input
DerivedOptogenetic protein kinase A is a light-controlled, multi-component switch built around the Cry2-Cib photodimerizing pair to investigate localized protein kinase A function. Upon light stimulation, a low-constitutive-activity protein kinase A catalytic subunit is translocated to a Cib-defined subcellular site, where kinase activity is restored.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationHeterodimerizationHeterodimerizationlight-induced protein translocationlight-induced protein translocationTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
Implementation requires a multi-component construct architecture based on Cry2 and Cib, with Cib localized to a chosen subcellular region and a low-constitutive-activity protein kinase A catalytic subunit fused for light-dependent recruitment. The evidence supports subcellular targeting and domain fusion logic, but does not specify expression system, linker design, cofactors, or illumination parameters.
The supplied evidence is limited to a design/mechanism description and does not report kinetics, dynamic range, reversibility, wavelength details, or validation across cell types. Independent replication is not evident from the provided sources.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
A photoactivated adenylate cyclase was engineered for expression at specific subcellular locations to investigate localized cAMP signaling.
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
Light activation of the photoactivated adenylate cyclase produces large increases in cellular cAMP levels and downstream signaling events.
Upon activation with light, large increases in cellular cAMP levels are observed resulting in down-stream signaling events.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug optogenetic-protein-kinase-a
I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
Source:
mechanismsupports
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
Source:
tool developmentsupports
The thesis reports development of two optogenetic proteins to investigate localized functions of protein kinase A and cAMP.
To this end, I have developed two optogenetic proteins for investigating the localized functions of 1) protein kinase A and 2) its second messenger cAMP.
Source:
Comparisons
Source-backed strengths
The design provides light-triggered subcellular translocation through the Cry2-Cib photodimerizing system and couples localization to restoration of protein kinase A activity. The evidence directly supports spatially defined activation logic, but does not provide quantitative performance metrics in the supplied material.
Source:
In order to investigate localized cAMP signaling, a photoactivated adenylate cyclase was engineered to be expressed at specific subcellular locations.
Compared with fusion proteins with large N-terminal anchors
optogenetic protein kinase A and fusion proteins with large N-terminal anchors address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Compared with LOVpep/ePDZb
optogenetic protein kinase A and LOVpep/ePDZb address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with tandem-dimer nano (tdnano)
optogenetic protein kinase A and tandem-dimer nano (tdnano) address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Ranked Citations
- 1.