Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules
The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. Whe...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2008-02, Vol.319 (5867), p.1247-1250 |
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| creator | Hu, Junjie Shibata, Yoko Voss, Christiane Shemesh, Tom Li, Zongli Coughlin, Margaret Kozlov, Michael M Rapoport, Tom A Prinz, William A |
| description | The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (~15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER. |
| doi_str_mv | 10.1126/science.1153634 |
| format | Article |
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Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (~15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1153634</identifier><identifier>PMID: 18309084</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Biological and medical sciences ; Biopolymers - chemistry ; Biopolymers - metabolism ; Cell membranes ; Cell structures and functions ; Cellular biology ; Cercopithecus aethiops ; COS Cells ; Curvature ; Detergents ; Endoplasmic Reticulum - chemistry ; Endoplasmic Reticulum - metabolism ; Endoplasmic Reticulum - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes - chemistry ; Intracellular Membranes - ultrastructure ; Lipid Bilayers ; Lipids ; Membrane Lipids - chemistry ; Membrane proteins ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - metabolism ; Membranes ; Microscopy, Electron ; Miscellaneous ; Models, Biological ; Molecular and cellular biology ; Molecular Sequence Data ; Mutant Proteins - chemistry ; Mutant Proteins - metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Proteins ; Proteolipids - chemistry ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Yeasts</subject><ispartof>Science (American Association for the Advancement of Science), 2008-02, Vol.319 (5867), p.1247-1250</ispartof><rights>Copyright 2008 American Association for the Advancement of Science</rights><rights>2008 INIST-CNRS</rights><rights>Copyright © 2008, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-16cd5009b2538c3d0aa43b98891a9fcb4696aa010d4d1065416f7e2909e216e23</citedby><cites>FETCH-LOGICAL-c526t-16cd5009b2538c3d0aa43b98891a9fcb4696aa010d4d1065416f7e2909e216e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20053486$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20053486$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2883,2884,27923,27924,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20162301$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18309084$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hu, Junjie</creatorcontrib><creatorcontrib>Shibata, Yoko</creatorcontrib><creatorcontrib>Voss, Christiane</creatorcontrib><creatorcontrib>Shemesh, Tom</creatorcontrib><creatorcontrib>Li, Zongli</creatorcontrib><creatorcontrib>Coughlin, Margaret</creatorcontrib><creatorcontrib>Kozlov, Michael M</creatorcontrib><creatorcontrib>Rapoport, Tom A</creatorcontrib><creatorcontrib>Prinz, William A</creatorcontrib><title>Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (~15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biopolymers - chemistry</subject><subject>Biopolymers - metabolism</subject><subject>Cell membranes</subject><subject>Cell structures and functions</subject><subject>Cellular biology</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Curvature</subject><subject>Detergents</subject><subject>Endoplasmic Reticulum - chemistry</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endoplasmic Reticulum - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Intracellular Membranes - chemistry</subject><subject>Intracellular Membranes - ultrastructure</subject><subject>Lipid Bilayers</subject><subject>Lipids</subject><subject>Membrane Lipids - chemistry</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Membranes</subject><subject>Microscopy, Electron</subject><subject>Miscellaneous</subject><subject>Models, Biological</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutant Proteins - chemistry</subject><subject>Mutant Proteins - metabolism</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteolipids - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Yeasts</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EotvCmRMQVYJb6Pgz9hGtCq20CATt2XKcSZtVEi92jMR_j6uNAHHhNBq93zzNzCPkBYV3lDJ1kfyAs8fSSK64eEQ2FIysDQP-mGwAuKo1NPKEnKa0Byia4U_JCdUcDGixIbtPOLXRzVh9iWHBYU5V6KvlHqvLuQuH0aVp8NVXXAafxzxV13OXPVZXw919vc3xh1tyxOomt3nE9Iw86d2Y8Plaz8jth8ub7VW9-_zxevt-V3vJ1FJT5TtZdmmZ5NrzDpwTvDVaG-pM71uhjHIOKHSio6CkoKpvkBkwyKhCxs_I26PvIYbvGdNipyF5HMdyR8jJNsDLO5T4L8hANpw2soDn_4D7kONcjrCMcqmNkKpAF0fIx5BSxN4e4jC5-NNSsA9x2DUOu8ZRJl6ttrmdsPvDr_8vwJsVcMm7sS9J-CH95hhQxTjQwr08cvu0hPiXDpIL_bDa66Peu2DdXSwet9_KNAfQSirJ-C-Zy6Sw</recordid><startdate>20080229</startdate><enddate>20080229</enddate><creator>Hu, Junjie</creator><creator>Shibata, Yoko</creator><creator>Voss, Christiane</creator><creator>Shemesh, Tom</creator><creator>Li, Zongli</creator><creator>Coughlin, Margaret</creator><creator>Kozlov, Michael M</creator><creator>Rapoport, Tom A</creator><creator>Prinz, William A</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>FBQ</scope><scope>IQODW</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20080229</creationdate><title>Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules</title><author>Hu, Junjie ; Shibata, Yoko ; Voss, Christiane ; Shemesh, Tom ; Li, Zongli ; Coughlin, Margaret ; Kozlov, Michael M ; Rapoport, Tom A ; Prinz, William A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-16cd5009b2538c3d0aa43b98891a9fcb4696aa010d4d1065416f7e2909e216e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biopolymers - chemistry</topic><topic>Biopolymers - metabolism</topic><topic>Cell membranes</topic><topic>Cell structures and functions</topic><topic>Cellular biology</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Curvature</topic><topic>Detergents</topic><topic>Endoplasmic Reticulum - chemistry</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endoplasmic Reticulum - ultrastructure</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hu, Junjie</au><au>Shibata, Yoko</au><au>Voss, Christiane</au><au>Shemesh, Tom</au><au>Li, Zongli</au><au>Coughlin, Margaret</au><au>Kozlov, Michael M</au><au>Rapoport, Tom A</au><au>Prinz, William A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2008-02-29</date><risdate>2008</risdate><volume>319</volume><issue>5867</issue><spage>1247</spage><epage>1250</epage><pages>1247-1250</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (~15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>18309084</pmid><doi>10.1126/science.1153634</doi><tpages>4</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 2008-02, Vol.319 (5867), p.1247-1250 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acid Sequence Amino acids Animals Biological and medical sciences Biopolymers - chemistry Biopolymers - metabolism Cell membranes Cell structures and functions Cellular biology Cercopithecus aethiops COS Cells Curvature Detergents Endoplasmic Reticulum - chemistry Endoplasmic Reticulum - metabolism Endoplasmic Reticulum - ultrastructure Fundamental and applied biological sciences. Psychology Hydrophobic and Hydrophilic Interactions Intracellular Membranes - chemistry Intracellular Membranes - ultrastructure Lipid Bilayers Lipids Membrane Lipids - chemistry Membrane proteins Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Membranes Microscopy, Electron Miscellaneous Models, Biological Molecular and cellular biology Molecular Sequence Data Mutant Proteins - chemistry Mutant Proteins - metabolism Protein Structure, Quaternary Protein Structure, Tertiary Proteins Proteolipids - chemistry Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Yeasts |
| title | Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules |
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