Pflügers Archiv - European Journal of Physiology

, Volume 456, Issue 6, pp 1199–1206

Discovery of protein-palmitoylating enzymes

Signaling and Cell Physiology

DOI: 10.1007/s00424-008-0465-x

Cite this article as:
Tsutsumi, R., Fukata, Y. & Fukata, M. Pflugers Arch - Eur J Physiol (2008) 456: 1199. doi:10.1007/s00424-008-0465-x

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.

Keywords

Protein palmitoylationDHHC proteinLipid modificationProtein targetingPalmitoyl-acyl transferase

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Ryouhei Tsutsumi
    • 1
  • Yuko Fukata
    • 1
    • 2
  • Masaki Fukata
    • 1
    • 2
  1. 1.Division of Membrane Physiology, Department of Cell PhysiologyNational Institute for Physiological SciencesOkazakiJapan
  2. 2.PRESTOJapan Science and Technology AgencyTokyoJapan