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Updated: Jun 3, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)
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DHHC palmitoyl transferases: substrate interactions and (patho)physiology.

Jennifer Greaves1, Luke H Chamberlain

  • 1Centre for Integrative Physiology, University of Edinburgh, Edinburgh, UK.

Trends in Biochemical Sciences
|March 11, 2011
PubMed
Summary

S-palmitoylation, a key protein modification, is regulated by DHHC enzymes. Understanding these enzymes and their targets is crucial for cell function and disease research.

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Last Updated: Jun 3, 2026

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • S-palmitoylation is a reversible post-translational modification impacting protein function.
  • This process influences membrane association, trafficking, and localization of diverse cellular proteins.

Purpose of the Study:

  • To explore the role of aspartate-histidine-histidine-cysteine (DHHC) palmitoyl transferases in protein modification.
  • To understand the specificity of DHHC-substrate pairings and their regulatory mechanisms.

Main Methods:

  • Review of recent studies on DHHC proteins and their substrates.
  • Analysis of the known functions and implications of S-palmitoylation.

Main Results:

  • Over 20 DHHC proteins are encoded in mammalian genomes.
  • DHHC proteins are critical regulators of cellular functions, physiology, and pathophysiology.

Conclusions:

  • Identifying DHHC-substrate interactions is a major focus in current research.
  • DHHC-mediated palmitoylation significantly impacts cellular processes and disease states.