Phosphorylation of diacylglycerol kinase-zeta by protein kinase C regulates its interaction with the PDZ domain of syntrophins

Elias Daher
Diacylglycerol kinase-zeta (DGK-zeta) attenuates diacylglycerol (DAG) signaling by converting it into phosphatidic acid (PA). DGK-zeta binds via its C-terminus, which contains a PSD-95/ Discs-Large/ZO-1 (PDZ)-binding motif, to a family of PDZ domain-containing scaffold proteins called syntrophins. Previous studies showed that some PDZ-mediated interactions are regulated by phosphorylation of the C-terminal PDZ-binding motif, however, to my knowledge, there are no published reports which demonstrate that a phosphorylation outside of this motif regulates PDZ interactions. Here, I...
This data repository is not currently reporting usage information. For information on how your repository can submit usage information, please see our documentation.