Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin–proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding ex...
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| Veröffentlicht in: | Nature cell biology 2002-02, Vol.4 (2), p.134-139 |
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| creator | Jarosch, Ernst Taxis, Christof Volkwein, Corinna Bordallo, Javier Finley, Daniel Wolf, Dieter H. Sommer, Thomas |
| description | Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin–proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome. |
| doi_str_mv | 10.1038/ncb746 |
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It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb746</identifier><identifier>PMID: 11813000</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adenosine triphosphatase ; Adenosine Triphosphatases - metabolism ; Biodegradation ; Biomedical and Life Sciences ; Cancer Research ; Carboxypeptidases - genetics ; Carboxypeptidases - metabolism ; Cathepsin A ; Cell Biology ; Cell Cycle Proteins - metabolism ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Developmental Biology ; Endoplasmic Reticulum - metabolism ; Experiments ; Fungal Proteins - metabolism ; Life Sciences ; Molecular Weight ; Nuclear Pore Complex Proteins ; Nuclear Proteins - metabolism ; Nucleocytoplasmic Transport Proteins ; Peptide Hydrolases - metabolism ; Physiological aspects ; Proteasome Endopeptidase Complex ; Protein Transport - physiology ; Proteins ; Proteolysis ; Saccharomyces cerevisiae Proteins - metabolism ; Stem Cells ; Substrates ; Ubiquitin - metabolism ; Ubiquitin-proteasome system ; Upstream ; Valosin Containing Protein ; Vesicular Transport Proteins</subject><ispartof>Nature cell biology, 2002-02, Vol.4 (2), p.134-139</ispartof><rights>Springer Nature Limited 2002</rights><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-399e5d73ebbcf7a53c541d1146e9258d21fe25e244b9681cefd9367cc5b447503</citedby><cites>FETCH-LOGICAL-c473t-399e5d73ebbcf7a53c541d1146e9258d21fe25e244b9681cefd9367cc5b447503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ncb746$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ncb746$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27902,27903,41466,42535,51296</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11813000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jarosch, Ernst</creatorcontrib><creatorcontrib>Taxis, Christof</creatorcontrib><creatorcontrib>Volkwein, Corinna</creatorcontrib><creatorcontrib>Bordallo, Javier</creatorcontrib><creatorcontrib>Finley, Daniel</creatorcontrib><creatorcontrib>Wolf, Dieter H.</creatorcontrib><creatorcontrib>Sommer, Thomas</creatorcontrib><title>Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin–proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. 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Academic</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jarosch, Ernst</au><au>Taxis, Christof</au><au>Volkwein, Corinna</au><au>Bordallo, Javier</au><au>Finley, Daniel</au><au>Wolf, Dieter H.</au><au>Sommer, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>4</volume><issue>2</issue><spage>134</spage><epage>139</epage><pages>134-139</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin–proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11813000</pmid><doi>10.1038/ncb746</doi><tpages>6</tpages></addata></record> |
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| subjects | Adenosine triphosphatase Adenosine Triphosphatases - metabolism Biodegradation Biomedical and Life Sciences Cancer Research Carboxypeptidases - genetics Carboxypeptidases - metabolism Cathepsin A Cell Biology Cell Cycle Proteins - metabolism Cell Membrane - chemistry Cell Membrane - metabolism Developmental Biology Endoplasmic Reticulum - metabolism Experiments Fungal Proteins - metabolism Life Sciences Molecular Weight Nuclear Pore Complex Proteins Nuclear Proteins - metabolism Nucleocytoplasmic Transport Proteins Peptide Hydrolases - metabolism Physiological aspects Proteasome Endopeptidase Complex Protein Transport - physiology Proteins Proteolysis Saccharomyces cerevisiae Proteins - metabolism Stem Cells Substrates Ubiquitin - metabolism Ubiquitin-proteasome system Upstream Valosin Containing Protein Vesicular Transport Proteins |
| title | Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48 |
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