TY - JOUR T1 - Endothelial Nitric-Oxide Synthase Reveals a New Face in G Protein Signaling JF - Molecular Pharmacology JO - Mol Pharmacol SP - 677 LP - 679 DO - 10.1124/mol.105.022038 VL - 69 IS - 3 AU - Matthew L. Bilodeau AU - Heidi E. Hamm Y1 - 2006/03/01 UR - http://molpharm.aspetjournals.org/content/69/3/677.abstract N2 - In this issue of Molecular Pharmacology, Andreeva et al. (p. 975) report a novel functional link between the heterotrimeric G protein Gα12 and endothelial nitric-oxide synthase (eNOS). Based on studies characterizing the interaction of Gα12 and the molecular chaperone Hsp90 and the interaction of eNOS and Hsp90, the group proposed an interaction between Gα12 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 Gα12 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 Gα12-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. ER -