Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases | Zendy

Ethan P. Marin | Zendy; Behrad Derakhshan | Zendy; TuKiet T. Lam | Zendy; Alberto Dávalos | Zendy; William C. Sessa | Zendy

Open Access

Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases

Author(s) -

Ethan P. Marin,

Behrad Derakhshan,

TuKiet T. Lam,

Alberto Dávalos,

William C. Sessa

Publication year - 2012

Publication title -

circulation research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.899

H-Index - 336

eISSN - 1524-4571

pISSN - 0009-7330

DOI - 10.1161/circresaha.112.269514

Subject(s) - cell , biochemistry , chemistry , microbiology and biotechnology , endothelial stem cell , biology , in vitro

Protein S-palmitoylation is the posttranslational attachment of a saturated 16-carbon palmitic acid to a cysteine side chain via a thioester bond. Palmitoylation can affect protein localization, trafficking, stability, and function. The extent and roles of palmitoylation in endothelial cell (EC) biology is not well-understood, partly because of technological limits on palmitoylprotein detection.

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