Source 1primary paper2018Scholarly Commons (University of Pennsylvania)
Toolkit/optogenetic RGS2
optogenetic RGS2
Also known as: opto-RGS2
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Optogenetic RGS2 (opto-RGS2) is an engineered light-responsive RGS2-based protein tool created to study calcium encoding in Gq-protein signaling. It uses light-induced heterodimerization to recruit an RGS2 domain to the membrane, where it interacts with its cognate G protein and modulates calcium oscillatory behavior.
Usefulness & Problems
Why this is useful
opto-RGS2 is useful for experimentally controlling Gq-linked calcium oscillation dynamics with light in an engineered cell-line context. In the cited study, it enabled optical re-creation of calcium oscillation patterns that independently varied a single waveform component, supporting analysis of calcium encoding.
Source:
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Source:
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
Problem solved
This tool addresses the problem of perturbing Gq-protein signaling with temporal precision to test how specific features of calcium oscillations are generated and regulated. The reported application was to study how RGS2 functions within the signaling circuit controlling periodic and stochastic calcium responses.
Source:
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
recombinationsignalingInput: Light
Implementation Constraints
The reported implementation combined an engineered opto-RGS2 cell line with a light-induced heterodimerization system that recruits the RGS2 domain to the membrane. The study also used mathematical modeling and custom hardware, but the supplied evidence does not specify cofactors, expression system details, or the exact heterodimerization pair.
The available evidence is limited to a single cited study in an engineered cell line and does not report broader validation across cell types, organisms, or in vivo settings. Practical performance details such as light wavelength, kinetics, dynamic range, and construct architecture are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically engineered cell line, and custom hardware, the authors optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using a mathematical model, an optogenetically-engineered cell line, and custom hardware, we optically re-created patterns of calcium oscillations that independently varied a single waveform component.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug optogenetic-rgs2
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
Source:
functional effectsupports
Using the engineered opto-RGS2 cell line, RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Using our engineered opto-RGS2 cell line, we revealed that RGS2 reduced periodicity and stochasticity of G-protein coupled calcium oscillations and acted as a feedback regulator in this signaling circuit.
Source:
mechanismsupports
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
A light-induced hetero-dimerization system was engineered to recruit the RGS2 domain to the membrane where it interacted with its cognate G protein.
Source:
tool developmentsupports
The authors developed optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
First, we created optogenetic RGS2 (opto-RGS2) for studying calcium encoding.
Source:
Comparisons
Source-backed strengths
The tool was specifically engineered for light-dependent membrane recruitment of an RGS2 domain to its site of action on cognate G protein signaling. In the reported engineered cell line, opto-RGS2 reduced periodicity and stochasticity of G-protein-coupled calcium oscillations and functioned as a feedback regulator, demonstrating functional control over oscillatory signaling.
Ranked Citations
- 1.