Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 7, Issue 7, Pages 1378-1388Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M800069-MCP200
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Funding
- NIMH NIH HHS [R21 MH071400, MH071400-01] Funding Source: Medline
- NINDS NIH HHS [R21 NS053638, NS053638-01] Funding Source: Medline
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Protein palmitoylation is the post-translational addition of the 16-carbon fatty acid palmitate to specific cysteine residues by a labile thioester linkage. Palmitoylation is mediated by a family of at least 23 palmitoyl acyltransferases (PATs) characterized by an Asp-His-His-Cys (DHHC) motif. Many palmitoylated proteins have been identified, but PAT-substrate relationships are mostly unknown. Here we present a method called palmitoylcysteine isolation capture and analysis (or PICA) to identify PAT-substrate relationships in a living vertebrate system and demonstrate its effectiveness by identifying CKAP4/p63 as a substrate of DHHC2, a putative tumor suppressor.
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