Protein kinase D1 (PKD1) phosphorylation on Ser²⁰³ by type I p21-activated kinase (PAK) regulates PKD1 localization.

ABSTRACT: Although PKC-mediated phosphorylation of protein kinase D1 (PKD1) has been extensively characterized, little is known about PKD1 regulation by other upstream kinases. Here we report that stimulation of epithelial or fibroblastic cells with G protein-coupled receptor agonists, including angiotensin II or bombesin, induced rapid and persistent PKD1 phosphorylation at Ser²⁰³, a highly conserved residue located within the PKD1 N-terminal domain. Exposure to PKD or PKC family inhibitors did not prevent PKD1 phosphorylation at Ser²⁰³, indicating that it is not mediated by autophosphorylation. In contrast, several lines of evidence indicated that the phosphorylation of PKD1 at Ser²⁰³ is mediated by kinases of the class I PAK subfamily, specifically 1) exposing cel

SUBMITTER: Chang JK 

PROVIDER: S-EPMC5465480 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature