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 06

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摘要

Heat shock protein 20 (HSP20) has cardioprotective qualities, which are triggered by 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 duanyu1529 and PKD1 can both phosphorylate HSP20 on serine 16 but that duanyu1529 is the most dominant. Copyright Â© 2015 John Wiley & Sons, Ltd.

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

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