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Molecular Pharmacology Fast Forward
First published on December 23, 2005; DOI: 10.1124/mol.105.022038

0026-895X/06/6903-677-679$20.00
Mol Pharmacol 69:677-679, 2006

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Perspective

Endothelial Nitric-Oxide Synthase Reveals a New Face in G Protein Signaling

Matthew L. Bilodeau, and Heidi E. Hamm

Department of Pharmacology (M.L.B., H.E.H.) and Department of Medicine, Division of Cardiovascular Medicine (M.L.B.), Vanderbilt University Medical Center, Nashville, Tennessee

In this issue of Molecular Pharmacology, Andreeva et al. (p. 975) report a novel functional link between the heterotrimeric G protein G{alpha}12 and endothelial nitric-oxide synthase (eNOS). Based on studies characterizing the interaction of G{alpha}12 and the molecular chaperone Hsp90 and the interaction of eNOS and Hsp90, the group proposed an interaction between G{alpha}12 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{alpha}12 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{alpha}12-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.

Received December 22, 2005; accepted December 23, 2005

Address correspondence to: Heidi E. Hamm, Vanderbilt University Medical Center, 2200 Pierce Ave., 442 Robinson Research Building, Nashville, TN 37232-6600. E-mail: heidi.hamm{at}vanderbilt.edu.


Related articles in MolPharm:

Novel Mechanisms of G Protein-Dependent Regulation of Endothelial Nitric-Oxide Synthase
Alexandra V. Andreeva, Rita Vaiskunaite, Mikhail A. Kutuzov, Jasmina Profirovic, Randal A. Skidgel, and Tatyana Voyno-Yasenetskaya
MolPharm 2006 69: 975-982. [Abstract] [Full Text]  



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