Dataset Information

Direct analysis of IFITM3 S-fatty-acylation, part 2

ABSTRACT: Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and another site adjacent to a transmembrane domain (C105). We directly identified the S-fatty-acylation sites of IFITM3, and further demonstrated that the highly conserved Cys residues are primarily modified by palmitic acid.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell, Kidney

SUBMITTER: Emmanuelle Thinon

LAB HEAD: Howard C. Hang

PROVIDER: PXD008401 | Pride | 2018-03-28

REPOSITORIES: Pride

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Publications

Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.

Thinon Emmanuelle E Fernandez Joseph P JP Molina Henrik H Hang Howard C HC

Journal of proteome research 20180406 5

S-Fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryotes and is important in mammalian physiology and human diseases. While chemical labeling methods have improved the detection and enrichment of S-fatty-acylated proteins, mapping sites of modification a ...[more]

PMID: 29575903

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