| pubmed-article:19801377 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0751973 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0175659 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0349674 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:19801377 | lifeskim:mentions | umls-concept:C0222045 | lld:lifeskim |
| pubmed-article:19801377 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19801377 | pubmed:dateCreated | 2010-1-7 | lld:pubmed |
| pubmed-article:19801377 | pubmed:abstractText | Protein S-acylation (palmitoylation), a reversible post-translational modification, is critically involved in regulating protein subcellular localization, activity, stability, and multimeric complex assembly. However, proteome scale characterization of S-acylation has lagged far behind that of phosphorylation, and global analysis of the localization of S-acylated proteins within different membrane domains has not been reported. Here we describe a novel proteomics approach, designated palmitoyl protein identification and site characterization (PalmPISC), for proteome scale enrichment and characterization of S-acylated proteins extracted from lipid raft-enriched and non-raft membranes. In combination with label-free spectral counting quantitation, PalmPISC led to the identification of 67 known and 331 novel candidate S-acylated proteins as well as the localization of 25 known and 143 novel candidate S-acylation sites. Palmitoyl acyltransferases DHHC5, DHHC6, and DHHC8 appear to be S-acylated on three cysteine residues within a novel CCX(7-13)C(S/T) motif downstream of a conserved Asp-His-His-Cys cysteine-rich domain, which may be a potential mechanism for regulating acyltransferase specificity and/or activity. S-Acylation may tether cytoplasmic acyl-protein thioesterase-1 to membranes, thus facilitating its interaction with and deacylation of membrane-associated S-acylated proteins. Our findings also suggest that certain ribosomal proteins may be targeted to lipid rafts via S-acylation, possibly to facilitate regulation of ribosomal protein activity and/or dynamic synthesis of lipid raft proteins in situ. In addition, bioinformatics analysis suggested that S-acylated proteins are highly enriched within core complexes of caveolae and tetraspanin-enriched microdomains, both cholesterol-rich membrane structures. The PalmPISC approach and the large scale human S-acylated protein data set are expected to provide powerful tools to facilitate our understanding of the functions and mechanisms of protein S-acylation. | lld:pubmed |
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| pubmed-article:19801377 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19801377 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19801377 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19801377 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19801377 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19801377 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19801377 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19801377 | pubmed:issn | 1535-9484 | lld:pubmed |
| pubmed-article:19801377 | pubmed:author | pubmed-author:SteenHannoH | lld:pubmed |
| pubmed-article:19801377 | pubmed:author | pubmed-author:YangWeiW | lld:pubmed |
| pubmed-article:19801377 | pubmed:author | pubmed-author:FreemanMichae... | lld:pubmed |
| pubmed-article:19801377 | pubmed:author | pubmed-author:Di... | lld:pubmed |
| pubmed-article:19801377 | pubmed:author | pubmed-author:KirchnerMarcM | lld:pubmed |
| pubmed-article:19801377 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19801377 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:19801377 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19801377 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19801377 | pubmed:pagination | 54-70 | lld:pubmed |
| pubmed-article:19801377 | pubmed:dateRevised | 2011-7-19 | lld:pubmed |
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