Discovery of protein-palmitoylating enzymes

Ryouhei Tsutsumi, Yuko Fukata, Masaki Fukata

Research output: Contribution to journalReview article

68 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1199-1206
Number of pages8
JournalPflugers Archiv European Journal of Physiology
Volume456
Issue number6
DOIs
Publication statusPublished - 2008 Sep 1
Externally publishedYes

Keywords

  • DHHC protein
  • Lipid modification
  • Palmitoyl-acyl transferase
  • Protein palmitoylation
  • Protein targeting

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Physiology (medical)

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