Key result
PKD1 phosphorylates the cardioprotective chaperone HSP20 on serine 16, although PKA remains the most dominant kinase for this site.
This study identifies HSP20 as a novel substrate for PKD1, providing new insights into the molecular mechanisms of cardioprotection.
No immediate clinical implications; leaves open PKD1 targeting for HSP20-mediated cardioprotection beyond PKA.
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.
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Sin et al. (2015) studied this question. PKD1 activity modulation (pharmacological or siRNA) was evaluated on HSP20 phosphorylation. PKD1 phosphorylates the cardioprotective chaperone HSP20 on serine 16, although PKA remains the most dominant kinase for this site.
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