Bat3 promotes the membrane integration of tail-anchored proteins

The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of cell science 2010-07, Vol.123 (13), p.2170-2178
Hauptverfasser: Leznicki, Pawel, Clancy, Anne, Schwappach, Blanche, High, Stephen
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2178
container_issue 13
container_start_page 2170
container_title Journal of cell science
container_volume 123
creator Leznicki, Pawel
Clancy, Anne
Schwappach, Blanche
High, Stephen
description The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61β, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61β, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins.
doi_str_mv 10.1242/jcs.066738
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2886740</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>733353793</sourcerecordid><originalsourceid>FETCH-LOGICAL-c467t-7030e2ffb881eb143c3a85637101c242be73e3d358b1881af71acb85b4f333e33</originalsourceid><addsrcrecordid>eNpVkMtOwzAQRS0EglLY8AGQHRJSwM44cbJBQMVLQmIBXVuOO2ldJXGxXST-HlcpCFZezJl7PYeQE0YvWcazq6X2l7QoBJQ7ZMS4EGnFQOySEaUZS6sc4IAcer-klIqsEvvkIKM5KxivRuTmTgVIVs52NqBPwgKTDrvaqR4T0wecOxWM7RPbJEGZNlW9XliHs81KQNP7I7LXqNbj8fYdk-nD_fvkKX15fXye3L6kmhcipIICxaxp6rJkWDMOGlSZFyAYZToeUaMAhBnkZc0iohrBlK7LvOYNQJzAmFwPuat13eFMYx-cauXKmU65L2mVkf8nvVnIuf2UWVkWgtMYcL4NcPZjjT7IzniNbRtPtWsvRezJQVSbqouB1M5677D5bWFUbozLaFwOxiN8-vdfv-iP4gicDUCjrFRzZ7ycvmWUAWUbAZzDN_9xhc4</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733353793</pqid></control><display><type>article</type><title>Bat3 promotes the membrane integration of tail-anchored proteins</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><source>Company of Biologists</source><creator>Leznicki, Pawel ; Clancy, Anne ; Schwappach, Blanche ; High, Stephen</creator><creatorcontrib>Leznicki, Pawel ; Clancy, Anne ; Schwappach, Blanche ; High, Stephen</creatorcontrib><description>The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61β, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61β, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.066738</identifier><identifier>PMID: 20516149</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Cytosol - metabolism ; Humans ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Qa-SNARE Proteins - genetics ; Qa-SNARE Proteins - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; SEC Translocation Channels ; Signal Transduction - physiology</subject><ispartof>Journal of cell science, 2010-07, Vol.123 (13), p.2170-2178</ispartof><rights>2010. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-7030e2ffb881eb143c3a85637101c242be73e3d358b1881af71acb85b4f333e33</citedby><cites>FETCH-LOGICAL-c467t-7030e2ffb881eb143c3a85637101c242be73e3d358b1881af71acb85b4f333e33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20516149$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leznicki, Pawel</creatorcontrib><creatorcontrib>Clancy, Anne</creatorcontrib><creatorcontrib>Schwappach, Blanche</creatorcontrib><creatorcontrib>High, Stephen</creatorcontrib><title>Bat3 promotes the membrane integration of tail-anchored proteins</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61β, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61β, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Humans</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - genetics</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - metabolism</subject><subject>Qa-SNARE Proteins - genetics</subject><subject>Qa-SNARE Proteins - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>SEC Translocation Channels</subject><subject>Signal Transduction - physiology</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkMtOwzAQRS0EglLY8AGQHRJSwM44cbJBQMVLQmIBXVuOO2ldJXGxXST-HlcpCFZezJl7PYeQE0YvWcazq6X2l7QoBJQ7ZMS4EGnFQOySEaUZS6sc4IAcer-klIqsEvvkIKM5KxivRuTmTgVIVs52NqBPwgKTDrvaqR4T0wecOxWM7RPbJEGZNlW9XliHs81KQNP7I7LXqNbj8fYdk-nD_fvkKX15fXye3L6kmhcipIICxaxp6rJkWDMOGlSZFyAYZToeUaMAhBnkZc0iohrBlK7LvOYNQJzAmFwPuat13eFMYx-cauXKmU65L2mVkf8nvVnIuf2UWVkWgtMYcL4NcPZjjT7IzniNbRtPtWsvRezJQVSbqouB1M5677D5bWFUbozLaFwOxiN8-vdfv-iP4gicDUCjrFRzZ7ycvmWUAWUbAZzDN_9xhc4</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Leznicki, Pawel</creator><creator>Clancy, Anne</creator><creator>Schwappach, Blanche</creator><creator>High, Stephen</creator><general>The Company of Biologists Limited</general><general>Company of Biologists</general><scope>FBQ</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>20100701</creationdate><title>Bat3 promotes the membrane integration of tail-anchored proteins</title><author>Leznicki, Pawel ; Clancy, Anne ; Schwappach, Blanche ; High, Stephen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c467t-7030e2ffb881eb143c3a85637101c242be73e3d358b1881af71acb85b4f333e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cytosol - metabolism</topic><topic>Humans</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Transport Proteins - genetics</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Molecular Chaperones - genetics</topic><topic>Molecular Chaperones - metabolism</topic><topic>Qa-SNARE Proteins - genetics</topic><topic>Qa-SNARE Proteins - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>SEC Translocation Channels</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leznicki, Pawel</creatorcontrib><creatorcontrib>Clancy, Anne</creatorcontrib><creatorcontrib>Schwappach, Blanche</creatorcontrib><creatorcontrib>High, Stephen</creatorcontrib><collection>AGRIS</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>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leznicki, Pawel</au><au>Clancy, Anne</au><au>Schwappach, Blanche</au><au>High, Stephen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bat3 promotes the membrane integration of tail-anchored proteins</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>123</volume><issue>13</issue><spage>2170</spage><epage>2178</epage><pages>2170-2178</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61β, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61β, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins.</abstract><cop>England</cop><pub>The Company of Biologists Limited</pub><pmid>20516149</pmid><doi>10.1242/jcs.066738</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9533
ispartof Journal of cell science, 2010-07, Vol.123 (13), p.2170-2178
issn 0021-9533
1477-9137
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2886740
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; Company of Biologists
subjects Adenosine Triphosphate - metabolism
Animals
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Membrane - metabolism
Cytosol - metabolism
Humans
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Transport Proteins - genetics
Membrane Transport Proteins - metabolism
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Qa-SNARE Proteins - genetics
Qa-SNARE Proteins - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
SEC Translocation Channels
Signal Transduction - physiology
title Bat3 promotes the membrane integration of tail-anchored proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T18%3A40%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=Bat3%20promotes%20the%20membrane%20integration%20of%20tail-anchored%20proteins&rft.jtitle=Journal%20of%20cell%20science&rft.au=Leznicki,%20Pawel&rft.date=2010-07-01&rft.volume=123&rft.issue=13&rft.spage=2170&rft.epage=2178&rft.pages=2170-2178&rft.issn=0021-9533&rft.eissn=1477-9137&rft_id=info:doi/10.1242/jcs.066738&rft_dat=%3Cproquest_pubme%3E733353793%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=733353793&rft_id=info:pmid/20516149&rfr_iscdi=true