Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p
Secretory proteins are transported from the endoplasmic reticulum to the Golgi apparatus via COPII-coated intermediates. Yeast Erv29p is a transmembrane protein cycling between these compartments. It is conserved across species, with one ortholog found in each genome studied, including the surf-4 pr...
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| Veröffentlicht in: | Molecular membrane biology 2007-01, Vol.24 (4), p.259-268 |
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| container_title | Molecular membrane biology |
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| creator | Foley, Deirdre A. Sharpe, Hayley J. Otte, Stefan |
| description | Secretory proteins are transported from the endoplasmic reticulum to the Golgi apparatus via COPII-coated intermediates. Yeast Erv29p is a transmembrane protein cycling between these compartments. It is conserved across species, with one ortholog found in each genome studied, including the surf-4 protein in mammals. Yeast Erv29p acts as a receptor, loading a specific subset of soluble cargo, including glycosylated alpha factor pheromone precursor and carboxypeptidase Y, into vesicles. As the eukaryotic secretory pathway is highly conserved, mammalian surf-4 may perform a similar role in the transport of unknown substrates. Here we report the membrane topology of yeast Erv29p, which we solved by minimally invasive cysteine accessibility scanning using thiol-specific biotinylation and fluorescent labeling methods. Erv29p contains four transmembrane domains with both termini exposed to the cytosol. Two luminal loops may contain a recognition site for hydrophobic export signals on soluble cargo. |
| doi_str_mv | 10.1080/09687860601178518 |
| format | Article |
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Yeast Erv29p is a transmembrane protein cycling between these compartments. It is conserved across species, with one ortholog found in each genome studied, including the surf-4 protein in mammals. Yeast Erv29p acts as a receptor, loading a specific subset of soluble cargo, including glycosylated alpha factor pheromone precursor and carboxypeptidase Y, into vesicles. As the eukaryotic secretory pathway is highly conserved, mammalian surf-4 may perform a similar role in the transport of unknown substrates. Here we report the membrane topology of yeast Erv29p, which we solved by minimally invasive cysteine accessibility scanning using thiol-specific biotinylation and fluorescent labeling methods. Erv29p contains four transmembrane domains with both termini exposed to the cytosol. Two luminal loops may contain a recognition site for hydrophobic export signals on soluble cargo.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>coated vesicles</subject><subject>COPII</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Golgi</subject><subject>Golgi Apparatus - metabolism</subject><subject>Intracellular Membranes - chemistry</subject><subject>Membrane Proteins - chemistry</subject><subject>membrane topology</subject><subject>Molecular Probe Techniques</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>trafficking</subject><subject>Vesicular Transport Proteins</subject><issn>0968-7688</issn><issn>1464-5203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KAzEURoMoWn8ewI1k5W40yWSSDLqRUquguNF1yGSSdkqmGZOM0rc30oKI4Oou7vk-7j0AnGN0hZFA16hmgguGGMKYiwqLPTDBlNGiIqjcB5PvfcGZEEfgOMYVQogyRg_BEeaZoIJMwMuz6Zug1gYmP3jnFxvoLUxLA8269YNTse80DCZ1enRjnyk4927RwZRDcfAhQat08gHOwgeph1NwYJWL5mw3T8Db_ex1-lA8vcwfp3dPhaYcpYLXlagV0RXBiogGt6wSWrAWW8KRJa1liFNSly03WihWlQ1VVCFLG45ZTXl5Ai63vUPw76OJSfZd1Ma5_Iofo-SoIpRgmkG8BXXwMQZj5RC6XoWNxEh-W5R_LObMxa58bHrT_iR22jJwuwW6tfWhV58-uFYmtXE-2CxGd1GW__Xf_IovjXJpqVUwcuXHsM7i_rnuC8GMkaY</recordid><startdate>20070101</startdate><enddate>20070101</enddate><creator>Foley, Deirdre A.</creator><creator>Sharpe, Hayley J.</creator><creator>Otte, Stefan</creator><general>Informa UK Ltd</general><general>Taylor & Francis</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>7X8</scope></search><sort><creationdate>20070101</creationdate><title>Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p</title><author>Foley, Deirdre A. ; Sharpe, Hayley J. ; Otte, Stefan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-79589a2c521a28b1d658c86d1f270f2df6074293d7ec8a653b4a4a0f4b7169473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>coated vesicles</topic><topic>COPII</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Golgi</topic><topic>Golgi Apparatus - metabolism</topic><topic>Intracellular Membranes - chemistry</topic><topic>Membrane Proteins - chemistry</topic><topic>membrane topology</topic><topic>Molecular Probe Techniques</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>trafficking</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Foley, Deirdre A.</creatorcontrib><creatorcontrib>Sharpe, Hayley J.</creatorcontrib><creatorcontrib>Otte, Stefan</creatorcontrib><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><jtitle>Molecular membrane biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Foley, Deirdre A.</au><au>Sharpe, Hayley J.</au><au>Otte, Stefan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p</atitle><jtitle>Molecular membrane biology</jtitle><addtitle>Mol Membr Biol</addtitle><date>2007-01-01</date><risdate>2007</risdate><volume>24</volume><issue>4</issue><spage>259</spage><epage>268</epage><pages>259-268</pages><issn>0968-7688</issn><eissn>1464-5203</eissn><abstract>Secretory proteins are transported from the endoplasmic reticulum to the Golgi apparatus via COPII-coated intermediates. 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| fulltext | fulltext |
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| ispartof | Molecular membrane biology, 2007-01, Vol.24 (4), p.259-268 |
| issn | 0968-7688 1464-5203 |
| language | eng |
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| source | MEDLINE; Taylor & Francis; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Binding Sites coated vesicles COPII Endoplasmic reticulum Endoplasmic Reticulum - metabolism Golgi Golgi Apparatus - metabolism Intracellular Membranes - chemistry Membrane Proteins - chemistry membrane topology Molecular Probe Techniques Protein Structure, Tertiary Saccharomyces cerevisiae Proteins - chemistry trafficking Vesicular Transport Proteins |
| title | Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p |
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