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Data support the notion that the Galpha, but not Gbetagamma, arm of the Gi/o signalling is involved in TRPC4 activation and unveil new roles for RGS and RGS14 in fine-tuning TRPC4 activities.
The RBD region associates with the RGS domain region, producing an intramolecular interaction within RGS14 that enhances the GTPase activating function.
RGS14 can form complexes with GPCRs in cells that are dependent on Galpha(i/o) and these RGS14.Galpha(i1).GPCR complexes may be substrates for other signaling partners such as Ric-8A
RGS-14 may facilitate cognitive processing by modulating Cav1 channel-mediated intracellular divalent calcium ion Ca(2)+ transients.
RGS14 serves as a novel scaffold to integrate GTP-Binding Protein alpha Subunit and Ras/Raf/MAPkinase signalling events through the action of its GL domain.
We show that RGS14 is a component of mitotic asters formed in vitro from HeLa cell extracts and that depletion of RGS14 from cell extracts blocks aster formation.
NMR 1H, 13C and 15N resonances of the RGS domain (residues 56-207)
Study shows that RGS14 mRNA and protein are upregulated throughout postnatal mouse development, and RGS14 protein exhibits a dynamic localization pattern that is enriched in hippocampus and primary olfactory cortex in the adult mouse brain
Inactive Galpha(i1)-GDP enhances the affinity of RGS14 for H-Ras-GTP in live cells, resulting in a ternary signaling complex that is further regulated by G protein-coupled receptors.
Activation of the Rsg14-Galphai1-GDP signaling complex is regulated by Ric8.
These results demonstrate that RGS14 is a key regulator of signaling pathways linking synaptic plasticity in CA2 pyramidal neurons to hippocampal-based learning and memory but distinct from the canonical DG-CA3-CA1 circuit.
the RGS14 GoLoco domain discriminates among Galphai isoforms
RGS14 is found ubiquitously throughout the postimplantation period in mice
RGS14 activity towards heterotrimeric G-proteins, as either a GAP or a guanine nucleotide dissociation inhibitor, was unaffected by Rap binding.
Morphine activation of Mu opioid receptors RGS14 prevents G-protein-coupled receptor kinases from phosphorylating those residues required for receptor endocytosis.
The regulator of G-protein signaling 14a protein, regulates the temporal relations between the appearance of the guidance molecules and the acquisition of cellular motility by regulating E-cadherin levels.
This gene encodes a member of the regulator of G-protein signaling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.
regulator of G-protein signalling 14
, RAP1/RAP2-interacting protein
, rap1/rap2 interacting protein
, regulator of G-protein signaling 14
, Regulator of G-protein signaling 14
, regulator of G-protein signaling 14-like
, LOW QUALITY PROTEIN: regulator of G-protein signaling 14