Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method |
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| Authors: | Zhang Jun Planey Sonia L Ceballos Carolina Stevens Stanley M Keay Susan K Zacharias David A |
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| Affiliation: | From the ‡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 |
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| 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. |
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