Source 1primary paper2008Journal of Neurochemistry
Toolkit/Galpha(16gust44)
Galpha(16gust44)
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Galpha(16gust44) is a G protein chimera used in HEK293 cells as part of a multi-component signaling switch. It couples the sweet taste receptor heterodimer TAS1R2/TAS1R3 to an InsP3-dependent intracellular Ca2+ release pathway.
Usefulness & Problems
Why this is useful
This chimera is useful for redirecting output from the sweet taste receptor dimer TAS1R2/TAS1R3 into a Ca2+-based readout in HEK293 cells. The available evidence supports its use as a pathway-coupling component in cell-based signaling assays, but does not provide broader performance benchmarking.
Source:
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Problem solved
It addresses the problem of linking TAS1R2/TAS1R3 receptor activation to an InsP3-dependent Ca2+ release pathway in a heterologous HEK293 cell system. This enables receptor signaling to be monitored through intracellular calcium responses rather than relying on the receptor's native coupling context.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
The reported implementation context is HEK293 cells co-opting the sweet taste receptor heterodimer TAS1R2/TAS1R3 into an InsP3-dependent Ca2+ release pathway using the Galpha(16gust44) chimera. No additional practical details such as sequence design, expression strategy, stoichiometry, or delivery method are provided in the supplied evidence.
Evidence is limited to a single cited study and a narrow use case in HEK293 cells with TAS1R2/TAS1R3. The available material does not report quantitative performance, dynamic range, specificity relative to other GPCRs, construct architecture, or independent replication.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
Depletion of CIB1 by short-hairpin RNA increases the Ca2+ response of HEK293 cells to InsP3-generating ligands ATP, UTP, and carbachol.
Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
Approval Evidence
1 source1 linked approval claimfirst-pass slug galpha-16gust44
the G protein chimeras Galpha(16gust44) and Galpha(15i3)
Source:
pathway couplingsupports
In HEK293 cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway.
In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway
Source:
Comparisons
Source-backed strengths
The cited study explicitly identifies Galpha(16gust44) as a chimera that links TAS1R2/TAS1R3 to InsP3-dependent Ca2+ release in HEK293 cells. This provides direct evidence for functional pathway redirection in a defined mammalian expression system.
Ranked Citations
- 1.