ArticleCell biochemistry and function2015
Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1).
Article in Cell biochemistry and function, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Review
- Novel NUDCD1 gene variant predisposes to severe COVID-19 disease in Asians through modulation of antiviral DHX15- and MAVS-mediated signalling.Frontiers in immunology · 2025Article
- Mechano-growth factor E-domain modulates cardiac contractile function through 14-3-3 protein interactomes.Frontiers in physiology · 2022Article
- Role of ATP-Small Heat Shock Protein Interaction in Human Diseases.Frontiers in molecular biosciences · 2022Review
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- The Cardioprotective PKA-Mediated Hsp20 Phosphorylation Modulates Protein Associations Regulating Cytoskeletal Dynamics.International journal of molecular sciences · 2020Article
- A-Kinase Anchoring Protein-Lbc: A Molecular Scaffold Involved in Cardiac Protection.Journal of cardiovascular development and disease · 2018Review
- Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20).Cell stress & chaperones · 2016Article
- Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1).Cell biochemistry and function · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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.
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