Jason Fontana

TL;DR: It is shown that the serine/threonine protein kinase Akt (protein kinase B) can directly phosphorylate eNOS on serine 1179 and activate the enzyme, leading to NO production, whereas mutant eN OS (S1179A) is resistant to phosphorylation and activation by Akt.

TL;DR: It is demonstrated that stimulation of endothelial cells with vascular endothelial growth factor recruits eNOS and Akt to an adjacent region on the same domain of hsp90, thereby facilitating eN OS phosphorylation and enzyme activation.

TL;DR: Data show that Hsp 90 is essential for eNOS-dependent ·NO production and that inhibition of ATP-dependent conformational changes in Hsp90 uncouples eN OS activity and increases eNos-dependent O⨪2production.

TL;DR: Results show that the actions of CaM on eNOS dissociation from caveolin are facilitated in the presence of hsp90, and eNos enzymatic activity is also less sensitive to inhibition by the caveolin scaffolding peptide when eN OS is prebound to hSp90.

TL;DR: Hsp90, a molecular chaperone that is central to the cellular stress response, associates with survivin, an apoptosis inhibitor and essential regulator of mitosis, and this interaction involves the ATPase domain of Hsp90 and the survivin baculovirus inhibitor of apoptosis repeat.