Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inhibition of Galphaq-dependent PLC-beta1 activity by PKG and PKA is mediated by phosphorylation of RGS4 and GRK2.

American journal of physiology. Cell physiology - 1 Jan 2007

Huang Jiean, Zhou Huiping, Mahavadi Sunila, Sriwai Wimolpak, Murthy Karnam S

Abstract excerpt

In smooth muscle of the gut, G(q)-coupled receptor agonists activate preferentially PLC-beta1 to stimulate phosphoinositide (PI) hydrolysis and inositol 1,4,5-trisphosphate (IP(3)) generation and induce IP(3)-dependent Ca(2+) release. Inhibition of Ca(2+) mobilization by cAMP- (PKA) and cGMP-dependent (PKG) protein kinases reflects inhibition of PI hydrolysis by both kinases and PKG-specific inhibitory...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cyclic GMP-Dependent Protein Kinases
Share to GTP-Binding Protein alpha Subunits, Gq-G11

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isoproterenol

Share to Nitroprusside

Share to Phosphatidylinositols

Share to Phospholipase C beta

Share to RGS Proteins

Share to Stomach

Source

Identifiers

PMID: 16885398
DOI: 10.1152/ajpcell.00103.2006

Genes

RGS4
GRK2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibition of Galphaq-dependent PLC-beta1 activity by PKG and PKA is mediated by phosphorylation of RGS4 and GRK2.PMID 16885398Read ↗

Phosphorylation of GRK2 by PKA augments GRK2-mediated phosphorylation, internalization, and desensitization of VPAC2 receptors in smooth muscle.Semantic proximity Read ↗

Inhibition of Gαi activity by Gβγ is mediated by PI 3-kinase-γ- and cSrc-dependent tyrosine phosphorylation of Gαi and recruitment of RGS12.Semantic proximity Read ↗

Phosphorylation of GTP dissociation inhibitor by PKA negatively regulates RhoA.Semantic proximity Read ↗

cGMP-dependent protein kinase protects cGMP from hydrolysis by phosphodiesterase-5.Semantic proximity Read ↗

GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits.Semantic proximity Read ↗

Agonist- and protein kinase C-induced phosphorylation have similar functional consequences for gastrin-releasing peptide receptor signaling via Gq.Semantic proximity Read ↗

Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism.Semantic proximity Read ↗

Signalling by cGMP-dependent protein kinases.Semantic proximity Read ↗

PKA-mediated phosphorylation of the beta1-adrenergic receptor promotes Gs/Gi switching.Semantic proximity Read ↗

Muscarinic receptors stimulate AC2 by novel phosphorylation sites, whereas Gβγ subunits exert opposing effects depending on the G-protein source.Semantic proximity Read ↗

Phosphoinositide 3-kinase gamma: kinase-dependent and -independent activities in cardiovascular function and disease.Semantic proximity Read ↗

Characterization of the GRK2 binding site of Galphaq.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.