Global Analysis of Protein Palmitoylation in Yeast
Protein palmitoylation is a reversible lipid modification that regulates membrane tethering for key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking. Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unav...
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| Veröffentlicht in: | Cell 2006-06, Vol.125 (5), p.1003-1013 |
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| container_title | Cell |
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| creator | Roth, Amy F. Wan, Junmei Bailey, Aaron O. Sun, Beimeng Kuchar, Jason A. Green, William N. Phinney, Brett S. Yates, John R. Davis, Nicholas G. |
| description | Protein palmitoylation is a reversible lipid modification that regulates membrane tethering for key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking. Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unavailable, and first-example palmitoylation enzymes—i.e., protein acyltransferases (PATs)—were identified only recently. Here, we use a new proteomic methodology that purifies and identifies palmitoylated proteins to characterize the palmitoyl proteome of the yeast Saccharomyces cerevisiae. Thirty-five new palmitoyl proteins are identified, including many SNARE proteins and amino acid permeases as well as many other participants in cellular signaling and membrane trafficking. Analysis of mutant yeast strains defective for members of the DHHC protein family, a putative PAT family, allows a matching of substrate palmitoyl proteins to modifying PATs and reveals the DHHC family to be a family of diverse PAT specificities responsible for most of the palmitoylation within the cell. |
| doi_str_mv | 10.1016/j.cell.2006.03.042 |
| format | Article |
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Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unavailable, and first-example palmitoylation enzymes—i.e., protein acyltransferases (PATs)—were identified only recently. Here, we use a new proteomic methodology that purifies and identifies palmitoylated proteins to characterize the palmitoyl proteome of the yeast Saccharomyces cerevisiae. Thirty-five new palmitoyl proteins are identified, including many SNARE proteins and amino acid permeases as well as many other participants in cellular signaling and membrane trafficking. Analysis of mutant yeast strains defective for members of the DHHC protein family, a putative PAT family, allows a matching of substrate palmitoyl proteins to modifying PATs and reveals the DHHC family to be a family of diverse PAT specificities responsible for most of the palmitoylation within the cell.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2006.03.042</identifier><identifier>PMID: 16751107</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetyltransferases - metabolism ; Acyltransferases - genetics ; Acyltransferases - isolation & purification ; Acyltransferases - metabolism ; Mutation - genetics ; Palmitic Acid - metabolism ; Protein Processing, Post-Translational - physiology ; Proteome - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - analysis ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - isolation & purification ; Saccharomyces cerevisiae Proteins - metabolism ; Signal Transduction - physiology</subject><ispartof>Cell, 2006-06, Vol.125 (5), p.1003-1013</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c599t-5ad59d05575c02b4922f91125d802b2b80627aff434ebb89a2077571dcc8a0c13</citedby><cites>FETCH-LOGICAL-c599t-5ad59d05575c02b4922f91125d802b2b80627aff434ebb89a2077571dcc8a0c13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867406005150$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16751107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roth, Amy F.</creatorcontrib><creatorcontrib>Wan, Junmei</creatorcontrib><creatorcontrib>Bailey, Aaron O.</creatorcontrib><creatorcontrib>Sun, Beimeng</creatorcontrib><creatorcontrib>Kuchar, Jason A.</creatorcontrib><creatorcontrib>Green, William N.</creatorcontrib><creatorcontrib>Phinney, Brett S.</creatorcontrib><creatorcontrib>Yates, John R.</creatorcontrib><creatorcontrib>Davis, Nicholas G.</creatorcontrib><title>Global Analysis of Protein Palmitoylation in Yeast</title><title>Cell</title><addtitle>Cell</addtitle><description>Protein palmitoylation is a reversible lipid modification that regulates membrane tethering for key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking. Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unavailable, and first-example palmitoylation enzymes—i.e., protein acyltransferases (PATs)—were identified only recently. Here, we use a new proteomic methodology that purifies and identifies palmitoylated proteins to characterize the palmitoyl proteome of the yeast Saccharomyces cerevisiae. Thirty-five new palmitoyl proteins are identified, including many SNARE proteins and amino acid permeases as well as many other participants in cellular signaling and membrane trafficking. Analysis of mutant yeast strains defective for members of the DHHC protein family, a putative PAT family, allows a matching of substrate palmitoyl proteins to modifying PATs and reveals the DHHC family to be a family of diverse PAT specificities responsible for most of the palmitoylation within the cell.</description><subject>Acetyltransferases - metabolism</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - isolation & purification</subject><subject>Acyltransferases - metabolism</subject><subject>Mutation - genetics</subject><subject>Palmitic Acid - metabolism</subject><subject>Protein Processing, Post-Translational - physiology</subject><subject>Proteome - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - analysis</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - isolation & purification</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal Transduction - physiology</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1PwyAchonRuDn9BzyYnry1_qClQGJMzOJXYuIOevBEKKXKwopCZ7L_XpYtflz0RIDnfQK_F6FjDAUGXJ_NC22cKwhAXUBZQEV20BiDYHmFGdlFYwBBcl6zaoQOYpwDAKeU7qMRrhnFGNgYkRvnG-Wyy165VbQx8102C34wts9myi3s4FdODdb3WTp5NioOh2ivUy6ao-06QU_XV4_T2_z-4eZuenmfayrEkFPVUtECpYxqIE0lCOkExoS2PG1Jw6EmTHVdVVamabhQBBijDLdacwUalxN0sfG-LZuFabXph6CcfAt2ocJKemXl75vevsoX_yEJqWrgZRKcbgXBvy9NHOTCxvXIVG_8MsqaQwLF_yBmmDOelBNENqAOPsZguq_XYJDrTuRcrnNy3YmEUqZOUujk5z--I9sSEnC-AUya5oc1QUZtTa9Na4PRg2y9_cv_CU2knM4</recordid><startdate>20060602</startdate><enddate>20060602</enddate><creator>Roth, Amy F.</creator><creator>Wan, Junmei</creator><creator>Bailey, Aaron O.</creator><creator>Sun, Beimeng</creator><creator>Kuchar, Jason A.</creator><creator>Green, William N.</creator><creator>Phinney, Brett S.</creator><creator>Yates, John R.</creator><creator>Davis, Nicholas G.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060602</creationdate><title>Global Analysis of Protein Palmitoylation in Yeast</title><author>Roth, Amy F. ; Wan, Junmei ; Bailey, Aaron O. ; Sun, Beimeng ; Kuchar, Jason A. ; Green, William N. ; Phinney, Brett S. ; Yates, John R. ; Davis, Nicholas G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c599t-5ad59d05575c02b4922f91125d802b2b80627aff434ebb89a2077571dcc8a0c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acetyltransferases - metabolism</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - isolation & purification</topic><topic>Acyltransferases - metabolism</topic><topic>Mutation - genetics</topic><topic>Palmitic Acid - metabolism</topic><topic>Protein Processing, Post-Translational - physiology</topic><topic>Proteome - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - analysis</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - isolation & purification</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roth, Amy F.</creatorcontrib><creatorcontrib>Wan, Junmei</creatorcontrib><creatorcontrib>Bailey, Aaron O.</creatorcontrib><creatorcontrib>Sun, Beimeng</creatorcontrib><creatorcontrib>Kuchar, Jason A.</creatorcontrib><creatorcontrib>Green, William N.</creatorcontrib><creatorcontrib>Phinney, Brett S.</creatorcontrib><creatorcontrib>Yates, John R.</creatorcontrib><creatorcontrib>Davis, Nicholas G.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roth, Amy F.</au><au>Wan, Junmei</au><au>Bailey, Aaron O.</au><au>Sun, Beimeng</au><au>Kuchar, Jason A.</au><au>Green, William N.</au><au>Phinney, Brett S.</au><au>Yates, John R.</au><au>Davis, Nicholas G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Global Analysis of Protein Palmitoylation in Yeast</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2006-06-02</date><risdate>2006</risdate><volume>125</volume><issue>5</issue><spage>1003</spage><epage>1013</epage><pages>1003-1013</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Protein palmitoylation is a reversible lipid modification that regulates membrane tethering for key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking. Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unavailable, and first-example palmitoylation enzymes—i.e., protein acyltransferases (PATs)—were identified only recently. Here, we use a new proteomic methodology that purifies and identifies palmitoylated proteins to characterize the palmitoyl proteome of the yeast Saccharomyces cerevisiae. Thirty-five new palmitoyl proteins are identified, including many SNARE proteins and amino acid permeases as well as many other participants in cellular signaling and membrane trafficking. 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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Acetyltransferases - metabolism Acyltransferases - genetics Acyltransferases - isolation & purification Acyltransferases - metabolism Mutation - genetics Palmitic Acid - metabolism Protein Processing, Post-Translational - physiology Proteome - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - analysis Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - isolation & purification Saccharomyces cerevisiae Proteins - metabolism Signal Transduction - physiology |
| title | Global Analysis of Protein Palmitoylation in Yeast |
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