title: Proteomic analysis of fatty-acylated proteins.
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.
authors.affiliation: Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States.
authors.forename: Tao
authors.initials: T
authors.lastname: Peng
authors.affiliation: 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.
authors.forename: Emmanuelle
authors.initials: E
authors.lastname: Thinon
authors.affiliation: Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States. Electronic address: hhang@rockefeller.edu.
authors.forename: Howard C
authors.initials: HC
authors.lastname: Hang
mesh_terms: D000215:Acylation; D000818:Animals; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D005227:Fatty Acids; D011506:Proteins