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Originally published In Press as doi:10.1074/mcp.M800069-MCP200 on February 22, 2008.
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Molecular & Cellular Proteomics 7:1378-1388, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

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

Jun Zhang{ddagger}, Sonia L. Planey{ddagger}, Carolina Ceballos{ddagger}, Stanley M. Stevens, Jr.§, Susan K. Keay and David A. Zacharias{ddagger},||

From the {ddagger} The Whitney Laboratory, Department of Neuroscience, University of Florida, St. Augustine, Florida 32080, § Proteomics Core Facility, Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, Florida, 32610, and Veterans Affairs Medical Center, University of Maryland, Baltimore, Maryland 21201

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.

|| A Partner in Research with Nikon. To whom correspondence should be addressed: The Whitney Laboratory for Marine Bioscience, University of Florida, St. Augustine, Florida 32080. Tel.: 904-461-4021; Fax: 904-461-4052; E-mail: daz{at}whitney.ufl.edu


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