Premium
Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
Author(s) -
Sin Yuan Yan,
Baillie George S.
Publication year - 2015
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.3147
Subject(s) - pkd1 , phosphorylation , chaperone (clinical) , heat shock protein , serine , kinase , protein kinase a , chemistry , microbiology and biotechnology , biochemistry , biology , medicine , genetics , gene , pathology , polycystic kidney disease , kidney
Heat shock protein 20 (HSP20) has cardioprotective qualities, which are triggered by PKA phosphorylation. PKD1 is also a binding partner for HSP20, and this prompted us to investigate whether the chaperone was a substrate for PKD1. We delineate the PKD1 binding sites on HSP20 and show for the first time HSP20 is a substrate for PKD1. Phosphorylation of HSP20 by PKD1 is diminished by pharmacological or siRNA reduction of PKD1 activity and is enhanced following PKD1 activation. Our results suggest that both PKA and PKD1 can both phosphorylate HSP20 on serine 16 but that PKA is the most dominant. © 2016 The Authors. Cell Biochemistry and Function published by John Wiley & Sons, Ltd.