The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
Misfolded secretory proteins are transported across the endoplasmic reticulum (ER) membrane into the cytosol for degradation by proteasomes. A large fraction of proteasomes in a cell is associated with the ER membrane. We show here that binding of proteasomes to ER membranes is salt sensitive, ATP d...
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| Veröffentlicht in: | The EMBO journal 2005-07, Vol.24 (13), p.2284-2293 |
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| creator | Kalies, Kai-Uwe Allan, Susanne Sergeyenko, Tatiana Kröger, Heike Römisch, Karin |
| description | Misfolded secretory proteins are transported across the endoplasmic reticulum (ER) membrane into the cytosol for degradation by proteasomes. A large fraction of proteasomes in a cell is associated with the ER membrane. We show here that binding of proteasomes to ER membranes is salt sensitive, ATP dependent, and mediated by the 19S regulatory particle. The base of the 19S particle, which contains six AAA‐ATPases, binds to microsomal membranes with high affinity, whereas the 19S lid complex binds weakly. We demonstrate that ribosomes and proteasomes compete for binding to the ER membrane and have similar affinities for their receptor. Ribosomes bind to the protein conducting channel formed by the Sec61 complex in the ER membrane. We co‐precipitated subunits of the Sec61 complex with ER‐associated proteasome 19S particles, and found that proteoliposomes containing only the Sec61 complex retained proteasome binding activity. Collectively, our data suggest that the Sec61 channel is a principal proteasome receptor in the ER membrane. |
| doi_str_mv | 10.1038/sj.emboj.7600731 |
| format | Article |
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A large fraction of proteasomes in a cell is associated with the ER membrane. We show here that binding of proteasomes to ER membranes is salt sensitive, ATP dependent, and mediated by the 19S regulatory particle. The base of the 19S particle, which contains six AAA‐ATPases, binds to microsomal membranes with high affinity, whereas the 19S lid complex binds weakly. We demonstrate that ribosomes and proteasomes compete for binding to the ER membrane and have similar affinities for their receptor. Ribosomes bind to the protein conducting channel formed by the Sec61 complex in the ER membrane. We co‐precipitated subunits of the Sec61 complex with ER‐associated proteasome 19S particles, and found that proteoliposomes containing only the Sec61 complex retained proteasome binding activity. Collectively, our data suggest that the Sec61 channel is a principal proteasome receptor in the ER membrane.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7600731</identifier><identifier>PMID: 15973433</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adenosine Triphosphatases - metabolism ; Animals ; ATP ; Dogs ; EMBO20 ; EMBO31 ; endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; ER-associated degradation ; Intracellular Membranes - metabolism ; Membrane Proteins - metabolism ; Membrane Transport Proteins ; Membranes ; Microsomes - metabolism ; proteasome ; Proteasome Endopeptidase Complex - metabolism ; Protein Binding ; Protein Folding ; protein translocation ; Protein Transport ; Ribosomes - metabolism ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; SEC Translocation Channels ; Sec61 channel ; Translocation</subject><ispartof>The EMBO journal, 2005-07, Vol.24 (13), p.2284-2293</ispartof><rights>European Molecular Biology Organization 2005</rights><rights>Copyright © 2005 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Jul 6, 2005</rights><rights>Copyright © 2005, European Molecular Biology Organization 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6701-119f6edbf9fa71cd7807bcb6a89c38bafddfd5338cfca626394d563e38849bac3</citedby><cites>FETCH-LOGICAL-c6701-119f6edbf9fa71cd7807bcb6a89c38bafddfd5338cfca626394d563e38849bac3</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/PMC1173161/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1173161/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/sj.emboj.7600731$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15973433$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kalies, Kai-Uwe</creatorcontrib><creatorcontrib>Allan, Susanne</creatorcontrib><creatorcontrib>Sergeyenko, Tatiana</creatorcontrib><creatorcontrib>Kröger, Heike</creatorcontrib><creatorcontrib>Römisch, Karin</creatorcontrib><title>The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Misfolded secretory proteins are transported across the endoplasmic reticulum (ER) membrane into the cytosol for degradation by proteasomes. A large fraction of proteasomes in a cell is associated with the ER membrane. We show here that binding of proteasomes to ER membranes is salt sensitive, ATP dependent, and mediated by the 19S regulatory particle. The base of the 19S particle, which contains six AAA‐ATPases, binds to microsomal membranes with high affinity, whereas the 19S lid complex binds weakly. We demonstrate that ribosomes and proteasomes compete for binding to the ER membrane and have similar affinities for their receptor. Ribosomes bind to the protein conducting channel formed by the Sec61 complex in the ER membrane. We co‐precipitated subunits of the Sec61 complex with ER‐associated proteasome 19S particles, and found that proteoliposomes containing only the Sec61 complex retained proteasome binding activity. Collectively, our data suggest that the Sec61 channel is a principal proteasome receptor in the ER membrane.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Animals</subject><subject>ATP</subject><subject>Dogs</subject><subject>EMBO20</subject><subject>EMBO31</subject><subject>endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>ER-associated degradation</subject><subject>Intracellular Membranes - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins</subject><subject>Membranes</subject><subject>Microsomes - metabolism</subject><subject>proteasome</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>protein translocation</subject><subject>Protein Transport</subject><subject>Ribosomes - metabolism</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>SEC Translocation Channels</subject><subject>Sec61 channel</subject><subject>Translocation</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</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>eNqFUUtv1DAYtBCILoU7F1DEgVsWO078uCCxVVkKpVyKECfLcb50HRJ7sROg_x7TrHYLEurJh3l45huEnhK8JJiKV7FbwlD7bskZxpySe2hBSobzAvPqPlrggpG8JEIeoUcxdhjjSnDyEB2RSnJaUrpAXy83kG2DH8G6bAzaxd4bPVrvMrPRzkGf1dY1cebo6AeI2eizMcnANX7b6zhYkwUYrZn6aciGlCj5wGP0oNV9hCe79xh9fnt6efIuP_-0Pjt5c54bxjHJCZEtg6ZuZas5MQ0XmNemZlpIQ0Wt26Zpm4pSYVqjWcGoLJuKUaBClLLWhh6j17PvdqoHaAy4VKNX22AHHa6V11b9jTi7UVf-hyIkXYyRZPByZxD89wniqAYbDfR9KuGnqJjAuJBFdScx-QnOS5aIL_4hdn4KLl1BEVkVqTcuEgnPJBN8jAHafWSC1Z91VezUzbpqt26SPL9d9SDYzZkIcib8tD1c32moTj-u3h_MyayNSeauINwK_f9Az2aN0-MUYP_hAc9n3MYRfu1hHb4pximv1JeLtVp9WK84v6CK09882-Aw</recordid><startdate>20050706</startdate><enddate>20050706</enddate><creator>Kalies, Kai-Uwe</creator><creator>Allan, Susanne</creator><creator>Sergeyenko, Tatiana</creator><creator>Kröger, Heike</creator><creator>Römisch, Karin</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</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>BKSAR</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>PCBAR</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>20050706</creationdate><title>The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane</title><author>Kalies, Kai-Uwe ; Allan, Susanne ; Sergeyenko, Tatiana ; Kröger, Heike ; Römisch, Karin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6701-119f6edbf9fa71cd7807bcb6a89c38bafddfd5338cfca626394d563e38849bac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adenosine Triphosphatases - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Kalies, Kai-Uwe</au><au>Allan, Susanne</au><au>Sergeyenko, Tatiana</au><au>Kröger, Heike</au><au>Römisch, Karin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2005-07-06</date><risdate>2005</risdate><volume>24</volume><issue>13</issue><spage>2284</spage><epage>2293</epage><pages>2284-2293</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Misfolded secretory proteins are transported across the endoplasmic reticulum (ER) membrane into the cytosol for degradation by proteasomes. A large fraction of proteasomes in a cell is associated with the ER membrane. We show here that binding of proteasomes to ER membranes is salt sensitive, ATP dependent, and mediated by the 19S regulatory particle. The base of the 19S particle, which contains six AAA‐ATPases, binds to microsomal membranes with high affinity, whereas the 19S lid complex binds weakly. We demonstrate that ribosomes and proteasomes compete for binding to the ER membrane and have similar affinities for their receptor. Ribosomes bind to the protein conducting channel formed by the Sec61 complex in the ER membrane. We co‐precipitated subunits of the Sec61 complex with ER‐associated proteasome 19S particles, and found that proteoliposomes containing only the Sec61 complex retained proteasome binding activity. 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| subjects | Adenosine Triphosphatases - metabolism Animals ATP Dogs EMBO20 EMBO31 endoplasmic reticulum Endoplasmic Reticulum - metabolism ER-associated degradation Intracellular Membranes - metabolism Membrane Proteins - metabolism Membrane Transport Proteins Membranes Microsomes - metabolism proteasome Proteasome Endopeptidase Complex - metabolism Protein Binding Protein Folding protein translocation Protein Transport Ribosomes - metabolism Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins SEC Translocation Channels Sec61 channel Translocation |
| title | The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane |
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