The Muscarinic Acetylcholine M₂ Receptor-Induced Nitration of p190A by eNOS Increases RhoA Activity in Cardiac Myocytes.

ABSTRACT: p190RhoGAP, which exists in two paralogs, p190RhoGAP-A (p190A) and p190RhoGAP-B (p190B), is a GTPase activating protein (GAP) contributing to the regulation of the cellular activity of RhoGTPases. Recent data showed that M₂ muscarinic acetylcholine receptor (M₂R) stimulation in neonatal rat cardiac myocytes (NRCM) induces the binding of p190RhoGAP to the long isoform of the regulator of G protein signaling 3 (RGS3L). This complex formation alters the substrate preference of p190RhoGAP from RhoA to Rac1. By analyzing carbachol-stimulated GAP activity, we show herein that p190A, but not p190B, alters its substrate preference in NRCM. Based on data that the RhoGAP activity of p190A in endothelial cells is diminished upon nitration by endothelial nitric oxide synthase (eN

SUBMITTER: Levay MK 

PROVIDER: S-EPMC10605742 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature