Work

Identification of CKAP4/p63 as a Major Substrate of the Palmitoyl Acyltransferase DHHC2, a Putative Tumor Suppressor, Using a Novel Proteomics Method

Year: 2008

Type: article

Abstract: 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 palmitoyl-cysteine 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.

Source: Molecular & Cellular Proteomics

DOI: 10.1074/mcp.m800069-mcp200

Authors: Jun Zhang, Sonia L. Planey, Carolina Ceballos, Stanley M. Stevens, Susan K. Keay, David A. Zacharias

Institutions: University of Florida, University of Maryland, Baltimore, Veterans Health Administration, Baltimore VA Medical Center

Language: English

Topic: Cancer, Lipids, and Metabolism

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institutes of Health, National Institute of Mental Health, National Institute of Neurological Disorders and Stroke