Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function
The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylatio...
Gespeichert in:
| Veröffentlicht in: | Molecular & cellular proteomics 2013-12, Vol.12 (12), p.3521-3531 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3531 |
|---|---|
| container_issue | 12 |
| container_start_page | 3521 |
| container_title | Molecular & cellular proteomics |
| container_volume | 12 |
| creator | Carrano, Andrea C. Bennett, Eric J. |
| description | The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylation targets have just started to emerge. Recent advances in ubiquitin-modified peptide enrichment have greatly increased the number of identified endogenous ubiquitylation targets, as well as the number of sites of ubiquitin attachment within these substrates. Herein we evaluate current strategies using mass-spectrometry-based proteomics to characterize ubiquitin and ubiquitin-like modifications. Using existing data, we describe the characteristics of the ubiquitin-modified proteome and discuss strategies for the biological interpretation of existing and future ubiquitin-based proteomic studies. |
| doi_str_mv | 10.1074/mcp.R113.029744 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3861705</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1535947620338226</els_id><sourcerecordid>1466376078</sourcerecordid><originalsourceid>FETCH-LOGICAL-c443t-9b5e38dab5f49d003fc97c70846dbd77a56b5ea23b159c77a06473091ad63f8c3</originalsourceid><addsrcrecordid>eNp1kcFPHSEQxompqdb27K3ZYy_7hAcLy8XEmFqbaGqM70xYmNVp3sITWJP-98WsfWkPPQ3z8eMbMh8hp4yuGFXibHK71T1jfEXXWglxQI5Zx7tWi16825-VPCIfcv5J6Zoy1b0nR2uuqFBKH5PbTcbw2JQnaDYDPs9YMLRT9Dgi-OYuxQJxgqbE5jYGLDEtGobmuuoxF5sxN1dzcAVj-EgOR7vN8OmtnpDN1deHy-v25se375cXN60TgpdWDx3w3tuhG4X2lPLRaeUU7YX0g1fKdrISds0H1mlXeyqF4lQz6yUfe8dPyPniu5uHCbyDUJLdml3CyaZfJlo0_94EfDKP8cXwXjJFu2rw5c0gxecZcjETZgfbrQ0Q52yYkJIrSVVf0bMFdSnmnGDcj2HUvIZgagjmNQSzhFBffP77d3v-z9YroBcA6o5eEJLJDiE48JjAFeMj_tf8N6ZYmCk</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1466376078</pqid></control><display><type>article</type><title>Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Carrano, Andrea C. ; Bennett, Eric J.</creator><creatorcontrib>Carrano, Andrea C. ; Bennett, Eric J.</creatorcontrib><description>The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylation targets have just started to emerge. Recent advances in ubiquitin-modified peptide enrichment have greatly increased the number of identified endogenous ubiquitylation targets, as well as the number of sites of ubiquitin attachment within these substrates. Herein we evaluate current strategies using mass-spectrometry-based proteomics to characterize ubiquitin and ubiquitin-like modifications. Using existing data, we describe the characteristics of the ubiquitin-modified proteome and discuss strategies for the biological interpretation of existing and future ubiquitin-based proteomic studies.</description><identifier>ISSN: 1535-9476</identifier><identifier>EISSN: 1535-9484</identifier><identifier>DOI: 10.1074/mcp.R113.029744</identifier><identifier>PMID: 23704779</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Gene Expression Regulation ; Glycylglycine - chemistry ; Glycylglycine - metabolism ; Homeostasis ; Humans ; Lysine - chemistry ; Lysine - metabolism ; Peptides - chemistry ; Peptides - genetics ; Peptides - metabolism ; Protein Processing, Post-Translational ; Proteolysis ; Proteome - chemistry ; Proteome - genetics ; Proteome - metabolism ; Signal Transduction - genetics ; Special Issue: Post-translational Modifications ; Substrate Specificity ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination ; Ubiquitins - genetics ; Ubiquitins - metabolism</subject><ispartof>Molecular & cellular proteomics, 2013-12, Vol.12 (12), p.3521-3531</ispartof><rights>2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-9b5e38dab5f49d003fc97c70846dbd77a56b5ea23b159c77a06473091ad63f8c3</citedby><cites>FETCH-LOGICAL-c443t-9b5e38dab5f49d003fc97c70846dbd77a56b5ea23b159c77a06473091ad63f8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3861705/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3861705/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23704779$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carrano, Andrea C.</creatorcontrib><creatorcontrib>Bennett, Eric J.</creatorcontrib><title>Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function</title><title>Molecular & cellular proteomics</title><addtitle>Mol Cell Proteomics</addtitle><description>The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylation targets have just started to emerge. Recent advances in ubiquitin-modified peptide enrichment have greatly increased the number of identified endogenous ubiquitylation targets, as well as the number of sites of ubiquitin attachment within these substrates. Herein we evaluate current strategies using mass-spectrometry-based proteomics to characterize ubiquitin and ubiquitin-like modifications. Using existing data, we describe the characteristics of the ubiquitin-modified proteome and discuss strategies for the biological interpretation of existing and future ubiquitin-based proteomic studies.</description><subject>Amino Acid Motifs</subject><subject>Gene Expression Regulation</subject><subject>Glycylglycine - chemistry</subject><subject>Glycylglycine - metabolism</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Lysine - chemistry</subject><subject>Lysine - metabolism</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteolysis</subject><subject>Proteome - chemistry</subject><subject>Proteome - genetics</subject><subject>Proteome - metabolism</subject><subject>Signal Transduction - genetics</subject><subject>Special Issue: Post-translational Modifications</subject><subject>Substrate Specificity</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitination</subject><subject>Ubiquitins - genetics</subject><subject>Ubiquitins - metabolism</subject><issn>1535-9476</issn><issn>1535-9484</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kcFPHSEQxompqdb27K3ZYy_7hAcLy8XEmFqbaGqM70xYmNVp3sITWJP-98WsfWkPPQ3z8eMbMh8hp4yuGFXibHK71T1jfEXXWglxQI5Zx7tWi16825-VPCIfcv5J6Zoy1b0nR2uuqFBKH5PbTcbw2JQnaDYDPs9YMLRT9Dgi-OYuxQJxgqbE5jYGLDEtGobmuuoxF5sxN1dzcAVj-EgOR7vN8OmtnpDN1deHy-v25se375cXN60TgpdWDx3w3tuhG4X2lPLRaeUU7YX0g1fKdrISds0H1mlXeyqF4lQz6yUfe8dPyPniu5uHCbyDUJLdml3CyaZfJlo0_94EfDKP8cXwXjJFu2rw5c0gxecZcjETZgfbrQ0Q52yYkJIrSVVf0bMFdSnmnGDcj2HUvIZgagjmNQSzhFBffP77d3v-z9YroBcA6o5eEJLJDiE48JjAFeMj_tf8N6ZYmCk</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>Carrano, Andrea C.</creator><creator>Bennett, Eric J.</creator><general>Elsevier Inc</general><general>The American Society for Biochemistry and Molecular Biology</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20131201</creationdate><title>Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function</title><author>Carrano, Andrea C. ; Bennett, Eric J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-9b5e38dab5f49d003fc97c70846dbd77a56b5ea23b159c77a06473091ad63f8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Motifs</topic><topic>Gene Expression Regulation</topic><topic>Glycylglycine - chemistry</topic><topic>Glycylglycine - metabolism</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Lysine - chemistry</topic><topic>Lysine - metabolism</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteolysis</topic><topic>Proteome - chemistry</topic><topic>Proteome - genetics</topic><topic>Proteome - metabolism</topic><topic>Signal Transduction - genetics</topic><topic>Special Issue: Post-translational Modifications</topic><topic>Substrate Specificity</topic><topic>Ubiquitin-Protein Ligases - genetics</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>Ubiquitination</topic><topic>Ubiquitins - genetics</topic><topic>Ubiquitins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carrano, Andrea C.</creatorcontrib><creatorcontrib>Bennett, Eric J.</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular & cellular proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carrano, Andrea C.</au><au>Bennett, Eric J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function</atitle><jtitle>Molecular & cellular proteomics</jtitle><addtitle>Mol Cell Proteomics</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>12</volume><issue>12</issue><spage>3521</spage><epage>3531</epage><pages>3521-3531</pages><issn>1535-9476</issn><eissn>1535-9484</eissn><abstract>The ubiquitin system is essential for the maintenance of proper protein homeostasis function across eukaryotic species. Although the general enzymatic architecture for adding and removing ubiquitin from substrates is well defined, methods for the comprehensive investigation of cellular ubiquitylation targets have just started to emerge. Recent advances in ubiquitin-modified peptide enrichment have greatly increased the number of identified endogenous ubiquitylation targets, as well as the number of sites of ubiquitin attachment within these substrates. Herein we evaluate current strategies using mass-spectrometry-based proteomics to characterize ubiquitin and ubiquitin-like modifications. Using existing data, we describe the characteristics of the ubiquitin-modified proteome and discuss strategies for the biological interpretation of existing and future ubiquitin-based proteomic studies.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>23704779</pmid><doi>10.1074/mcp.R113.029744</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1535-9476 |
| ispartof | Molecular & cellular proteomics, 2013-12, Vol.12 (12), p.3521-3531 |
| issn | 1535-9476 1535-9484 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3861705 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Motifs Gene Expression Regulation Glycylglycine - chemistry Glycylglycine - metabolism Homeostasis Humans Lysine - chemistry Lysine - metabolism Peptides - chemistry Peptides - genetics Peptides - metabolism Protein Processing, Post-Translational Proteolysis Proteome - chemistry Proteome - genetics Proteome - metabolism Signal Transduction - genetics Special Issue: Post-translational Modifications Substrate Specificity Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination Ubiquitins - genetics Ubiquitins - metabolism |
| title | Using the Ubiquitin-modified Proteome to Monitor Protein Homeostasis Function |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T14%3A32%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Using%20the%20Ubiquitin-modified%20Proteome%20to%20Monitor%20Protein%20Homeostasis%20Function&rft.jtitle=Molecular%20&%20cellular%20proteomics&rft.au=Carrano,%20Andrea%20C.&rft.date=2013-12-01&rft.volume=12&rft.issue=12&rft.spage=3521&rft.epage=3531&rft.pages=3521-3531&rft.issn=1535-9476&rft.eissn=1535-9484&rft_id=info:doi/10.1074/mcp.R113.029744&rft_dat=%3Cproquest_pubme%3E1466376078%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1466376078&rft_id=info:pmid/23704779&rft_els_id=S1535947620338226&rfr_iscdi=true |