Source 1primary paper2008Journal of Neurochemistry
Toolkit/Galpha(15i3)
Galpha(15i3)
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Galpha(15i3) is a G protein chimera reported in HEK293 cells as a pathway-linking component that couples the sweet taste receptor heterodimer TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway. It is described together with Galpha(16gust44) in receptor signaling assays.
Usefulness & Problems
Why this is useful
This chimera is useful as an assay-enabling coupling element that redirects TAS1R2/TAS1R3 signaling into an InsP3-dependent Ca2+ readout in HEK293 cells. The available evidence supports utility for cellular sweet receptor signaling measurements, but does not provide broader 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
Galpha(15i3) addresses the problem of linking TAS1R2/TAS1R3 activation to a measurable intracellular Ca2+ release pathway in HEK293 cells. This enables receptor signaling assays when native coupling is not directly configured for the desired InsP3-dependent readout.
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-used with the sweet taste receptor heterodimer TAS1R2/TAS1R3. The assay output is InsP3-dependent Ca2+ release, but the supplied evidence does not specify construct design, expression strategy, or additional cofactors.
Evidence is limited to a single cited study and a single cell context, HEK293 cells. No quantitative performance data, sequence or domain architecture, specificity analysis, or independent replication are provided in the supplied evidence.
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-15i3
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 reports that Galpha(15i3) links TAS1R2/TAS1R3 to an InsP3-dependent Ca2+ release pathway in HEK293 cells. This provides direct evidence for functional pathway coupling in a mammalian cell assay context.
Ranked Citations
- 1.