Potential Roles of Endoplasmic Reticulum Stress and Cellular Proteins Implicated in Diabesity

Figure 4

eNOS/Cav-1 interaction; it may be seen that eNOS is a homodimer limited to the Golgi apparatus and plasma membrane caveolae. In an inactive state, the caveolae protein is coupled to Cav-1, which reduces its action. Furthermore, when eNOS is phosphorylated by protein kinase C on Thr⁴⁹⁵, it inhibits contact with CaM. Inhibition of the enzyme can be achieved in a situation of oxidative stress caused in the aftermath of proline-rich tyrosine kinase 2- (PYK-2-) induced tyrosine phosphorylation of eNOS. Owing to cellular activation of eNOS, which is split from Cav-1, CaM can bind to the eNOS at Ser¹¹⁷⁷, thanks to Thr⁴⁹⁵ dephosphorylation, and produce EDRF.