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Protein lipidation.

Marissa J Nadolski1, Maurine E Linder

  • 1Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA.

The FEBS Journal
|September 26, 2007
PubMed
Summary
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This review explores S-palmitoylation, a lipid modification crucial for protein function. We focus on DHHC proteins that regulate palmitoylation of Ras proteins in yeast and mammalian cells.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteins undergo various lipid modifications, including S-palmitoylation, impacting their localization and function.
  • S-palmitoylation involves the reversible attachment of fatty acids to cysteine residues, influencing protein-membrane association, trafficking, and stability.

Purpose of the Study:

  • This review focuses on S-palmitoylation, a key post-translational modification.
  • It specifically examines the role of DHHC proteins in mediating palmitoylation of Ras proteins in yeast and mammalian systems.

Main Methods:

  • Literature review of S-palmitoylation and DHHC protein functions.
  • Analysis of studies on Ras protein palmitoylation in different cellular contexts.

Main Results:

Related Experiment Videos

  • S-palmitoylation is a dynamic process regulated by DHHC proteins.
  • DHHC proteins are integral membrane proteins responsible for catalyzing palmitoylation.
  • Palmitoylation of Ras proteins by specific DHHC enzymes affects their signaling and localization.

Conclusions:

  • DHHC proteins are central regulators of S-palmitoylation.
  • Understanding DHHC-mediated palmitoylation of Ras proteins is critical for deciphering cellular signaling pathways.
  • This modification impacts protein function, stability, and membrane interactions.