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Curr Opin Chem Biol. 2016 Feb;30:77-86. doi: 10.1016/j.cbpa.2015.11.008. Epub 2015 Dec 2.

Proteomic analysis of fatty-acylated proteins.

Author information

1
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States.
2
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States; The Crick Institute, 215 Euston Road, London NW1 2BE, United Kingdom.
3
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States. Electronic address: hhang@rockefeller.edu.

Abstract

Protein fatty-acylation in eukaryotes has been associated with many fundamental biological processes. However, the diversity, abundance and regulatory mechanisms of protein fatty-acylation in vivo remain to be explored. Herein, we review the proteomic analysis of fatty-acylated proteins, with a focus on N-myristoylation and S-palmitoylation. We then highlight major challenges and emerging methods for direct site identification, quantitation, and lipid structure characterization to understand the functions and regulatory mechanisms of fatty-acylated proteins in physiology and disease.

PMID:
26656971
PMCID:
PMC4731282
DOI:
10.1016/j.cbpa.2015.11.008
[Indexed for MEDLINE]
Free PMC Article

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