Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)

Cell Biochem Funct. 2015 Oct;33(7):421-6. doi: 10.1002/cbf.3147. Epub 2015 Oct 6.

Abstract

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.

Keywords: HSP20; PKA; PKD1; cardiac remodelling; peptide array.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Cells, Cultured
  • HSP20 Heat-Shock Proteins / metabolism*
  • Muscle Proteins / metabolism*
  • Myocytes, Cardiac / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Rats

Substances

  • HSP20 Heat-Shock Proteins
  • Muscle Proteins
  • Hspb6 protein, rat
  • protein kinase D
  • Protein Kinase C