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

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...

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Detalles Bibliográficos
Autores principales: Sin, Yuan Yan, Baillie, George S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Rapid Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4973849/
https://www.ncbi.nlm.nih.gov/pubmed/26443497
http://dx.doi.org/10.1002/cbf.3147
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author Sin, Yuan Yan
Baillie, George S.
author_facet Sin, Yuan Yan
Baillie, George S.
author_sort Sin, Yuan Yan
collection PubMed
description 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.
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spelling pubmed-49738492016-08-17 Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1) Sin, Yuan Yan Baillie, George S. Cell Biochem Funct Rapid Communication 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. John Wiley and Sons Inc. 2015-10-06 2015-10 /pmc/articles/PMC4973849/ /pubmed/26443497 http://dx.doi.org/10.1002/cbf.3147 Text en © 2016 The Authors. Cell Biochemistry and Function published by John Wiley & Sons, Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Rapid Communication
Sin, Yuan Yan
Baillie, George S.
Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title_full Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title_fullStr Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title_full_unstemmed Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title_short Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1)
title_sort heat shock protein 20 (hsp20) is a novel substrate for protein kinase d1 (pkd1)
topic Rapid Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4973849/
https://www.ncbi.nlm.nih.gov/pubmed/26443497
http://dx.doi.org/10.1002/cbf.3147
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