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Substrate recognition by the cell surface palmitoyl transferase DHHC5.

Jacqueline Howie1, Louise Reilly1, Niall J Fraser1

  • 1Division of Cardiovascular and Diabetes Medicine, Medical Research Institute, College of Medicine, Dentistry and Nursing, University of Dundee, Ninewells Hospital, Dundee DD1 9SY, United Kingdom;

Proceedings of the National Academy of Sciences of the United States of America
|November 26, 2014
PubMed
Summary

The cardiac enzyme DHHC5 palmitoylates phospholemman (PLM), a protein regulating the sodium pump. This palmitoylation at cysteine 40 inhibits the sodium pump, revealing a new regulatory mechanism in heart cells.

Keywords:
DHHCion transportpalmitoylationphospholemmansodium pump

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Area of Science:

  • Cardiovascular Biology
  • Molecular Cell Biology
  • Enzymology

Background:

  • Phospholemman (PLM) is a cardiac phosphoprotein that modulates the cardiac sodium pump.
  • Protein palmitoylation, catalyzed by Asp-His-His-Cys (DHHC) motif-containing enzymes, is a key post-translational modification.
  • DHHC5 is a cell surface palmitoyl acyltransferase with identified substrates being relatively few.

Purpose of the Study:

  • To investigate the role of DHHC5 in cardiac phosphoprotein regulation.
  • To identify and characterize the interaction between DHHC5 and PLM in ventricular myocytes.
  • To elucidate the functional consequences of PLM palmitoylation by DHHC5 on sodium pump activity.

Main Methods:

  • Quantitative analysis of DHHC isoform expression in ventricular muscle.
  • Coimmunoprecipitation assays to assess DHHC5-PLM interaction.
  • Overexpression and gene silencing experiments to determine DHHC5's role in PLM palmitoylation and sodium pump function.

Main Results:

  • DHHC5 is highly expressed in the heart and localizes to caveolin-enriched microdomains.
  • DHHC5 directly palmitoylates PLM at juxtamembrane cysteines (C40 and C42), with C40 being the primary site.
  • Palmitoylation of PLM at C40, but not C42, is essential for PLM-mediated inhibition of the sodium pump.

Conclusions:

  • An enzyme-substrate relationship between DHHC5 and PLM is established.
  • DHHC5-mediated PLM palmitoylation represents a novel mechanism for regulating cardiac sodium pump activity.
  • This interaction may involve PLM recruitment to phospholipids, leading to sodium pump inhibition.