Source 1primary paper2016Journal of Cell Science
Toolkit/Opto-Akt
Opto-Akt
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Opto-Akt is an optogenetic construct used to activate or target Akt with light in order to interrogate Akt-dependent signaling and subcellular localization. In adipocytes, its light-driven activity only partially triggered IRAP-pHluorin translocation, indicating that isolated Akt activation does not fully reproduce insulin-like trafficking responses.
Usefulness & Problems
Why this is useful
This construct is useful for separating Akt-specific contributions from broader PI3K-dependent insulin signaling using light as the input modality. The cited adipocyte study used it to test whether Akt activation alone is sufficient to drive insulin-responsive membrane trafficking.
Source:
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
Problem solved
Opto-Akt helps address the problem of causally testing whether Akt activation is sufficient to induce downstream trafficking events such as IRAP-pHluorin translocation. The available evidence indicates that this question is important because PI3K and Akt have distinct roles in adipocyte insulin action.
Problem links
Need conditional control of signaling activity
DerivedOpto-Akt is an optogenetic construct used to activate or target Akt with light to probe Akt-dependent control of subcellular localization and insulin-responsive signaling. In adipocytes, light-driven Opto-Akt activity only partially triggered IRAP-pHluorin translocation, indicating that Akt activation alone is insufficient to reproduce the full insulin-like trafficking response.
Need inducible protein relocalization or recruitment
DerivedOpto-Akt is an optogenetic construct used to activate or target Akt with light to probe Akt-dependent control of subcellular localization and insulin-responsive signaling. In adipocytes, light-driven Opto-Akt activity only partially triggered IRAP-pHluorin translocation, indicating that Akt activation alone is insufficient to reproduce the full insulin-like trafficking response.
Need precise spatiotemporal control with light input
DerivedOpto-Akt is an optogenetic construct used to activate or target Akt with light to probe Akt-dependent control of subcellular localization and insulin-responsive signaling. In adipocytes, light-driven Opto-Akt activity only partially triggered IRAP-pHluorin translocation, indicating that Akt activation alone is insufficient to reproduce the full insulin-like trafficking response.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
light-induced subcellular localizationlight-induced subcellular localizationspatially restricted akt activationspatially restricted akt activationTechniques
No technique tags yet.
Target processes
localizationsignalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: regulator
The tool is light controlled and was applied in adipocytes to assess IRAP-pHluorin translocation. The supplied evidence does not specify the photoreceptor system, required cofactors, expression strategy, or construct design details.
Evidence here is limited to a single cited study and a narrow readout, IRAP-pHluorin translocation in adipocytes. The supplied evidence does not provide quantitative performance details, kinetics, dynamic range, wavelength, construct architecture, or validation across additional cell types or Akt-dependent outputs.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug opto-akt
whereas Opto-Akt only partially triggered translocation
Source:
comparative effectsupports
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Source:
mechanistic conclusionsupports
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
Source:
spatial localization effectsupports
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Source:
Comparisons
Source-backed strengths
The main demonstrated strength is pathway dissection: Opto-Akt enabled direct comparison with Opto-PIP3 in the same biological context. Its partial effect on IRAP-pHluorin translocation provided evidence that Akt activation alone is insufficient for the full insulin-like response in adipocytes.
Source:
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Compared with BcLOV4 photoreceptor
Opto-Akt and BcLOV4 photoreceptor address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; same primary input modality: light
Compared with fusion proteins with large N-terminal anchors
Opto-Akt and fusion proteins with large N-terminal anchors address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; same primary input modality: light
Strengths here: looks easier to implement in practice.
Compared with NIR Rac1 biosensor
Opto-Akt and NIR Rac1 biosensor address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; same primary input modality: light
Ranked Citations
- 1.