A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome
The ubiquitin‐proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome—the protease responsible for the degradation of ubiquitylated proteins—several structural and functional questions remain unanswered....
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| Veröffentlicht in: | EMBO reports 2001-09, Vol.2 (9), p.821-828 |
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| creator | Davy, Anne Bello, Paul Thierry-Mieg, Nicolas Vaglio, Philippe Hitti, Joseph Doucette-Stamm, Lynn Thierry-Mieg, Danielle Reboul, Jérôme Boulton, Simon Walhout, Albertha J M Coux, Olivier Vidal, Marc |
| description | The ubiquitin‐proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome—the protease responsible for the degradation of ubiquitylated proteins—several structural and functional questions remain unanswered. To gain more insight into the assembly and function of the metazoan 26S proteasome, a two‐hybrid‐based protein interaction map was generated using 30
Caenorhabditis elegans
proteasome subunits. The results recapitulate interactions reported for other organisms and reveal new potential interactions both within the 19S regulatory complex and between the 19S and 20S subcomplexes. Moreover, novel potential proteasome interactors were identified, including an E3 ubiquitin ligase, transcription factors, chaperone proteins and other proteins not yet functionally annotated. By providing a wealth of novel biological hypotheses, this interaction map constitutes a framework for further analysis of the ubiquitin‐proteasome pathway in a multicellular organism amenable to both classical genetics and functional genomics. |
| doi_str_mv | 10.1093/embo-reports/kve184 |
| format | Article |
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Caenorhabditis elegans
proteasome subunits. The results recapitulate interactions reported for other organisms and reveal new potential interactions both within the 19S regulatory complex and between the 19S and 20S subcomplexes. Moreover, novel potential proteasome interactors were identified, including an E3 ubiquitin ligase, transcription factors, chaperone proteins and other proteins not yet functionally annotated. By providing a wealth of novel biological hypotheses, this interaction map constitutes a framework for further analysis of the ubiquitin‐proteasome pathway in a multicellular organism amenable to both classical genetics and functional genomics.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.1093/embo-reports/kve184</identifier><identifier>PMID: 11559592</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Caenorhabditis elegans - chemistry ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Databases as Topic ; Genetics ; Models, Molecular ; Open Reading Frames ; Peptide Hydrolases - chemistry ; Peptide Hydrolases - genetics ; Peptide Hydrolases - metabolism ; Plasmids - metabolism ; Polymerase Chain Reaction ; Proteasome Endopeptidase Complex ; Protein Binding ; Scientific Report ; Scientific Reports ; Transformation, Genetic ; Two-Hybrid System Techniques</subject><ispartof>EMBO reports, 2001-09, Vol.2 (9), p.821-828</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Sep 15, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6497-fe7666b52590730bce1a6ffecbd8fe214453d0ee67d647d0cdb32e37c9e51b263</citedby><cites>FETCH-LOGICAL-c6497-fe7666b52590730bce1a6ffecbd8fe214453d0ee67d647d0cdb32e37c9e51b263</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/PMC1084039/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1084039/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11559592$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Davy, Anne</creatorcontrib><creatorcontrib>Bello, Paul</creatorcontrib><creatorcontrib>Thierry-Mieg, Nicolas</creatorcontrib><creatorcontrib>Vaglio, Philippe</creatorcontrib><creatorcontrib>Hitti, Joseph</creatorcontrib><creatorcontrib>Doucette-Stamm, Lynn</creatorcontrib><creatorcontrib>Thierry-Mieg, Danielle</creatorcontrib><creatorcontrib>Reboul, Jérôme</creatorcontrib><creatorcontrib>Boulton, Simon</creatorcontrib><creatorcontrib>Walhout, Albertha J M</creatorcontrib><creatorcontrib>Coux, Olivier</creatorcontrib><creatorcontrib>Vidal, Marc</creatorcontrib><title>A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The ubiquitin‐proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome—the protease responsible for the degradation of ubiquitylated proteins—several structural and functional questions remain unanswered. To gain more insight into the assembly and function of the metazoan 26S proteasome, a two‐hybrid‐based protein interaction map was generated using 30
Caenorhabditis elegans
proteasome subunits. The results recapitulate interactions reported for other organisms and reveal new potential interactions both within the 19S regulatory complex and between the 19S and 20S subcomplexes. Moreover, novel potential proteasome interactors were identified, including an E3 ubiquitin ligase, transcription factors, chaperone proteins and other proteins not yet functionally annotated. By providing a wealth of novel biological hypotheses, this interaction map constitutes a framework for further analysis of the ubiquitin‐proteasome pathway in a multicellular organism amenable to both classical genetics and functional genomics.</description><subject>Animals</subject><subject>Caenorhabditis elegans - chemistry</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Databases as Topic</subject><subject>Genetics</subject><subject>Models, Molecular</subject><subject>Open Reading Frames</subject><subject>Peptide Hydrolases - chemistry</subject><subject>Peptide Hydrolases - genetics</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Plasmids - metabolism</subject><subject>Polymerase Chain Reaction</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Protein Binding</subject><subject>Scientific Report</subject><subject>Scientific Reports</subject><subject>Transformation, Genetic</subject><subject>Two-Hybrid System Techniques</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkU9v1DAQxSMEoqXwCZBQxIFbqB3HdnxBalftglSKBOXPzXKcya7bxA62U-i3x6tEW-DU01ia33sz45dlLzF6i5EgxzA0rvAwOh_D8c0t4Lp6lB3iiomCYF4_Xt5liX8cZM9CuEYIUcHrp9kBxpQKKsrD7PIkH72LYGyx1NzYCF7paJzNBzXmrsvjFvKVAuv8VjWtiSbk0MNG2ZCX7MvsoIIb4Hn2pFN9gBdLPcq-np9drd4XF5_WH1YnF4VmleBFB5wx1tCSCsQJajRgxboOdNPWHZS4qihpEQDjLat4i3TbkBII1wIobkpGjrJ3s-84NQO0Gmz0qpejN4Pyd9IpI__tWLOVG3crMaorREQyeLMYePdzghDlYIKGvlcW3BQkx5in0XUCX_8HXrvJ23ScLFFNMU-fnCAyQ9q7EDx0-00wkruw5C4suYQl57CS6tXfR9xrlnQSUM_AL9PD3UM85dnH08-E8CStZmlIKrsBf7_2g1ayKk4e9iN3rJ99ixkwIcLvfV_5G8k44VR-v1zLc766omT9TXLyB7dA1to</recordid><startdate>200109</startdate><enddate>200109</enddate><creator>Davy, Anne</creator><creator>Bello, Paul</creator><creator>Thierry-Mieg, Nicolas</creator><creator>Vaglio, Philippe</creator><creator>Hitti, Joseph</creator><creator>Doucette-Stamm, Lynn</creator><creator>Thierry-Mieg, Danielle</creator><creator>Reboul, Jérôme</creator><creator>Boulton, Simon</creator><creator>Walhout, Albertha J M</creator><creator>Coux, Olivier</creator><creator>Vidal, Marc</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200109</creationdate><title>A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome</title><author>Davy, Anne ; Bello, Paul ; Thierry-Mieg, Nicolas ; Vaglio, Philippe ; Hitti, Joseph ; Doucette-Stamm, Lynn ; Thierry-Mieg, Danielle ; Reboul, Jérôme ; Boulton, Simon ; Walhout, Albertha J M ; Coux, Olivier ; Vidal, Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6497-fe7666b52590730bce1a6ffecbd8fe214453d0ee67d647d0cdb32e37c9e51b263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Caenorhabditis elegans - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Davy, Anne</au><au>Bello, Paul</au><au>Thierry-Mieg, Nicolas</au><au>Vaglio, Philippe</au><au>Hitti, Joseph</au><au>Doucette-Stamm, Lynn</au><au>Thierry-Mieg, Danielle</au><au>Reboul, Jérôme</au><au>Boulton, Simon</au><au>Walhout, Albertha J M</au><au>Coux, Olivier</au><au>Vidal, Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2001-09</date><risdate>2001</risdate><volume>2</volume><issue>9</issue><spage>821</spage><epage>828</epage><pages>821-828</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>The ubiquitin‐proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome—the protease responsible for the degradation of ubiquitylated proteins—several structural and functional questions remain unanswered. To gain more insight into the assembly and function of the metazoan 26S proteasome, a two‐hybrid‐based protein interaction map was generated using 30
Caenorhabditis elegans
proteasome subunits. The results recapitulate interactions reported for other organisms and reveal new potential interactions both within the 19S regulatory complex and between the 19S and 20S subcomplexes. Moreover, novel potential proteasome interactors were identified, including an E3 ubiquitin ligase, transcription factors, chaperone proteins and other proteins not yet functionally annotated. By providing a wealth of novel biological hypotheses, this interaction map constitutes a framework for further analysis of the ubiquitin‐proteasome pathway in a multicellular organism amenable to both classical genetics and functional genomics.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11559592</pmid><doi>10.1093/embo-reports/kve184</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Caenorhabditis elegans - chemistry Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Databases as Topic Genetics Models, Molecular Open Reading Frames Peptide Hydrolases - chemistry Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Plasmids - metabolism Polymerase Chain Reaction Proteasome Endopeptidase Complex Protein Binding Scientific Report Scientific Reports Transformation, Genetic Two-Hybrid System Techniques |
| title | A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome |
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