Endothelial nitric-oxide synthase reveals a new face in G protein signaling.

Bilodeau ML, Hamm HE
Mol Pharmacol. 2006 69 (3): 677-9

PMID: 16377762 · DOI:10.1124/mol.105.022038

In this issue of Molecular Pharmacology, Andreeva et al. (p. 975) report a novel functional link between the heterotrimeric G protein G alpha12 and endothelial nitric-oxide synthase (eNOS). Based on studies characterizing the interaction of G alpha12 and the molecular chaperone Hsp90 and the interaction of eNOS and Hsp90, the group proposed an interaction between G alpha12 and eNOS and sought to determine the regulatory mechanisms, including the inferred dependence on Hsp90. Their experiments using an overexpression model lead to the observation that the cotransfection of G alpha12 and eNOS expression vectors increased overall eNOS expression. Additional studies in the overexpression model and in human umbilical vein endothelial cells (HUVEC) provide evidence for a mechanism that involves G alpha12-dependent stabilization of eNOS protein and possibly mRNA. These data present yet another paradigm by which heterotrimeric G proteins, through stabilization of target proteins, can regulate the activity of downstream signaling pathways.

MeSH Terms (10)

Animals Endothelium, Vascular Enzyme Stability GTP-Binding Protein alpha Subunits, G12-G13 HSP90 Heat-Shock Proteins Humans Nitric Oxide Synthase Type III RNA Stability Signal Transduction Transfection

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