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A more recent version of this article appeared on July 1, 2008.
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M800069-MCP200v1
7/7/1378    most recent
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Submitted on February 14, 2008
Accepted on February 22, 2008

Identification of CKAP4/p63 as a major substrate of the palmitoyl acyl transferase DHHC2, a putative tumor suppressor, using a novel proteomic method

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

The Whitney Laboratory University of Florida, St. Augustine, FL 32080

Corresponding Author: daz{at}whitney.ufl.edu

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 acyl transferases (PATs) characterized by an AspHisHisCys (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 physiologically important substrate of DHHC2, a putative tumor suppressor.


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