Discovery of protein-palmitoylating enzymes

Pflugers Arch. 2008 Sep;456(6):1199-206. doi: 10.1007/s00424-008-0465-x. Epub 2008 Jan 30.

Abstract

Posttranslational modification provides proteins with additional function and regulatory control beyond genomic information, allowing cells to maintain homeostasis and respond to extracellular signals. Protein palmitoylation, the common posttranslational modification with the lipid palmitate, plays a pivotal role in protein trafficking and function. Palmitoylation is unique in that it is reversible and dynamically regulated by specific extracellular signals. The reversible nature of protein palmitoylation enables proteins to shuttle between intracellular compartments upon extracellular signals. However, the molecular mechanisms of protein palmitoylation have long been elusive, mostly because the enzymes responsible for protein palmitoylation were unknown. Recently, genetically conserved DHHC family proteins have emerged as palmitoyl-acyl transferases. With the identification of specific enzymes for palmitoylated proteins, including H-Ras, PSD-95, and eNOS, the specificity and regulatory mechanism of DHHC enzymes are beginning to be clarified.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Enzymes / metabolism*
  • Gene Expression Regulation, Enzymologic / genetics
  • Gene Expression Regulation, Enzymologic / physiology
  • Humans
  • Palmitic Acids / metabolism*
  • Protein Processing, Post-Translational / physiology
  • Signal Transduction / physiology*
  • Substrate Specificity
  • Yeasts / enzymology
  • Yeasts / genetics

Substances

  • Enzymes
  • Palmitic Acids