Signaling and Cell Physiology

Pflügers Archiv - European Journal of Physiology

, Volume 456, Issue 6, pp 1199-1206

First online:

Discovery of protein-palmitoylating enzymes

  • Ryouhei TsutsumiAffiliated withDivision of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences
  • , Yuko FukataAffiliated withDivision of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological SciencesPRESTO, Japan Science and Technology Agency
  • , Masaki FukataAffiliated withDivision of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological SciencesPRESTO, Japan Science and Technology Agency Email author 

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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 palmitoylation DHHC protein Lipid modification Protein targeting Palmitoyl-acyl transferase