Sin, Y. Y. and Baillie, G. (2015) Heat Shock Protein 20 (HSP20) is a novel substrate for Protein Kinase D1 (PKD1). Cell Biochemistry and Function, 33(7), pp. 421-426. (doi: 10.1002/cbf.3147) (PMID:26443497) (PMCID:PMC4973849)
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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.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Baillie, Professor George and Sin, Dr Angie |
| Authors: | Sin, Y. Y., and Baillie, G. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health |
| Journal Name: | Cell Biochemistry and Function |
| Publisher: | Wiley |
| ISSN: | 0263-6484 |
| ISSN (Online): | 1099-0844 |
| Published Online: | 06 October 2015 |
| Copyright Holders: | Copyright © 2015 The Authors |
| First Published: | First published in Cell Biochemistry and Function 33(7):421-426 |
| Publisher Policy: | Reproduced under a Creative Commons License |
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