Translocation of proteins through the Sec61 and SecYEG channels
The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expres...
Gespeichert in:
| Veröffentlicht in: | Current opinion in cell biology 2009-08, Vol.21 (4), p.501-507 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 507 |
|---|---|
| container_issue | 4 |
| container_start_page | 501 |
| container_title | Current opinion in cell biology |
| container_volume | 21 |
| creator | Mandon, Elisabet C Trueman, Steven F Gilmore, Reid |
| description | The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expression, the transport channels undergo conformational changes to permit the export of lumenal domains and the integration of transmembrane spans. Novel insight into how these channels open during protein translocation has been provided by a combination of the analysis of new channel structures, biochemical characterization of translocation intermediates, molecular dynamics simulations, and in vivo and in vitro analysis of structure-based Sec61 and SecY mutants. |
| doi_str_mv | 10.1016/j.ceb.2009.04.010 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2916700</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0955067409000969</els_id><sourcerecordid>733578358</sourcerecordid><originalsourceid>FETCH-LOGICAL-c602t-eb356c5b200b6a40d6fab53d6e324871fc274644f0176f0c4b198c88cc97f9353</originalsourceid><addsrcrecordid>eNp9kk9r3DAQxUVpaLZJP0Avxaf2ZHdkyZJFIaGENC0Eckhy6EnI8jirrVfaSnYg374yu_TfIacR6DdPM3qPkLcUKgpUfNxUFruqBlAV8AoovCAr2kpVAqfwkqxANU0JQvJj8jqlDQAIqNUrckwVb0AJWJHzu2h8GoM1kwu-CEOxi2FC51MxrWOYH9a5YnGLVtDC-H45fb-8KuzaeI9jOiVHgxkTvjnUE3L_5fLu4mt5fXP17eLzdWnzk1OJHWuEbbo8aycMh14MpmtYL5DVvJV0sLXkgvMBqBQDWN5R1dq2tVbJQbGGnZCzve5u7rbYW_RTNKPeRbc18UkH4_S_N96t9UN41LWiQgJkgQ8HgRh-zpgmvXXJ4jgaj2FOWjLWyJY1bSbfP0vWIJUUTGaQ7kEbQ0oRh9_jUNCLQXqjs0F6MUgD19mg3PPu7z3-dBwcycCnPZA_Fx8dRp2sQ2-xdxHtpPvgnpU_-6_bjs47a8Yf-IRpE-bos02a6lRr0LdLQpaAgMrhUEKxX-KItNY</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20797637</pqid></control><display><type>article</type><title>Translocation of proteins through the Sec61 and SecYEG channels</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Mandon, Elisabet C ; Trueman, Steven F ; Gilmore, Reid</creator><creatorcontrib>Mandon, Elisabet C ; Trueman, Steven F ; Gilmore, Reid</creatorcontrib><description>The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expression, the transport channels undergo conformational changes to permit the export of lumenal domains and the integration of transmembrane spans. Novel insight into how these channels open during protein translocation has been provided by a combination of the analysis of new channel structures, biochemical characterization of translocation intermediates, molecular dynamics simulations, and in vivo and in vitro analysis of structure-based Sec61 and SecY mutants.</description><identifier>ISSN: 0955-0674</identifier><identifier>EISSN: 1879-0410</identifier><identifier>DOI: 10.1016/j.ceb.2009.04.010</identifier><identifier>PMID: 19450960</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Cell Membrane - metabolism ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Internal Medicine ; Lipid Bilayers - chemistry ; Membrane Proteins - chemistry ; Methanococcus - metabolism ; Models, Biological ; Molecular Conformation ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; SEC Translocation Channels ; Thermus - metabolism</subject><ispartof>Current opinion in cell biology, 2009-08, Vol.21 (4), p.501-507</ispartof><rights>Elsevier Ltd</rights><rights>2009 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-eb356c5b200b6a40d6fab53d6e324871fc274644f0176f0c4b198c88cc97f9353</citedby><cites>FETCH-LOGICAL-c602t-eb356c5b200b6a40d6fab53d6e324871fc274644f0176f0c4b198c88cc97f9353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0955067409000969$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19450960$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mandon, Elisabet C</creatorcontrib><creatorcontrib>Trueman, Steven F</creatorcontrib><creatorcontrib>Gilmore, Reid</creatorcontrib><title>Translocation of proteins through the Sec61 and SecYEG channels</title><title>Current opinion in cell biology</title><addtitle>Curr Opin Cell Biol</addtitle><description>The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expression, the transport channels undergo conformational changes to permit the export of lumenal domains and the integration of transmembrane spans. Novel insight into how these channels open during protein translocation has been provided by a combination of the analysis of new channel structures, biochemical characterization of translocation intermediates, molecular dynamics simulations, and in vivo and in vitro analysis of structure-based Sec61 and SecY mutants.</description><subject>Cell Membrane - metabolism</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Internal Medicine</subject><subject>Lipid Bilayers - chemistry</subject><subject>Membrane Proteins - chemistry</subject><subject>Methanococcus - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Conformation</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>SEC Translocation Channels</subject><subject>Thermus - metabolism</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kk9r3DAQxUVpaLZJP0Avxaf2ZHdkyZJFIaGENC0Eckhy6EnI8jirrVfaSnYg374yu_TfIacR6DdPM3qPkLcUKgpUfNxUFruqBlAV8AoovCAr2kpVAqfwkqxANU0JQvJj8jqlDQAIqNUrckwVb0AJWJHzu2h8GoM1kwu-CEOxi2FC51MxrWOYH9a5YnGLVtDC-H45fb-8KuzaeI9jOiVHgxkTvjnUE3L_5fLu4mt5fXP17eLzdWnzk1OJHWuEbbo8aycMh14MpmtYL5DVvJV0sLXkgvMBqBQDWN5R1dq2tVbJQbGGnZCzve5u7rbYW_RTNKPeRbc18UkH4_S_N96t9UN41LWiQgJkgQ8HgRh-zpgmvXXJ4jgaj2FOWjLWyJY1bSbfP0vWIJUUTGaQ7kEbQ0oRh9_jUNCLQXqjs0F6MUgD19mg3PPu7z3-dBwcycCnPZA_Fx8dRp2sQ2-xdxHtpPvgnpU_-6_bjs47a8Yf-IRpE-bos02a6lRr0LdLQpaAgMrhUEKxX-KItNY</recordid><startdate>20090801</startdate><enddate>20090801</enddate><creator>Mandon, Elisabet C</creator><creator>Trueman, Steven F</creator><creator>Gilmore, Reid</creator><general>Elsevier Ltd</general><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>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090801</creationdate><title>Translocation of proteins through the Sec61 and SecYEG channels</title><author>Mandon, Elisabet C ; Trueman, Steven F ; Gilmore, Reid</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-eb356c5b200b6a40d6fab53d6e324871fc274644f0176f0c4b198c88cc97f9353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Cell Membrane - metabolism</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Internal Medicine</topic><topic>Lipid Bilayers - chemistry</topic><topic>Membrane Proteins - chemistry</topic><topic>Methanococcus - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Conformation</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>SEC Translocation Channels</topic><topic>Thermus - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mandon, Elisabet C</creatorcontrib><creatorcontrib>Trueman, Steven F</creatorcontrib><creatorcontrib>Gilmore, Reid</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Current opinion in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mandon, Elisabet C</au><au>Trueman, Steven F</au><au>Gilmore, Reid</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Translocation of proteins through the Sec61 and SecYEG channels</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>2009-08-01</date><risdate>2009</risdate><volume>21</volume><issue>4</issue><spage>501</spage><epage>507</epage><pages>501-507</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expression, the transport channels undergo conformational changes to permit the export of lumenal domains and the integration of transmembrane spans. Novel insight into how these channels open during protein translocation has been provided by a combination of the analysis of new channel structures, biochemical characterization of translocation intermediates, molecular dynamics simulations, and in vivo and in vitro analysis of structure-based Sec61 and SecY mutants.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>19450960</pmid><doi>10.1016/j.ceb.2009.04.010</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0955-0674 |
| ispartof | Current opinion in cell biology, 2009-08, Vol.21 (4), p.501-507 |
| issn | 0955-0674 1879-0410 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2916700 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Cell Membrane - metabolism Endoplasmic reticulum Endoplasmic Reticulum - metabolism Escherichia coli - metabolism Escherichia coli Proteins - chemistry Internal Medicine Lipid Bilayers - chemistry Membrane Proteins - chemistry Methanococcus - metabolism Models, Biological Molecular Conformation Mutation Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Protein Transport SEC Translocation Channels Thermus - metabolism |
| title | Translocation of proteins through the Sec61 and SecYEG channels |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T13%3A39%3A38IST&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=Translocation%20of%20proteins%20through%20the%20Sec61%20and%20SecYEG%20channels&rft.jtitle=Current%20opinion%20in%20cell%20biology&rft.au=Mandon,%20Elisabet%20C&rft.date=2009-08-01&rft.volume=21&rft.issue=4&rft.spage=501&rft.epage=507&rft.pages=501-507&rft.issn=0955-0674&rft.eissn=1879-0410&rft_id=info:doi/10.1016/j.ceb.2009.04.010&rft_dat=%3Cproquest_pubme%3E733578358%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=20797637&rft_id=info:pmid/19450960&rft_els_id=S0955067409000969&rfr_iscdi=true |