Sar1 assembly regulates membrane constriction and ER export
The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to contro...
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| Veröffentlicht in: | The Journal of cell biology 2010-07, Vol.190 (1), p.115-128 |
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| container_title | The Journal of cell biology |
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| creator | Long, Kimberly R Yamamoto, Yasunori Baker, Adam L Watkins, Simon C Coyne, Carolyn B Conway, James F Aridor, Meir |
| description | The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). Sar1 activity was directed to liquid-disordered lipid phases. Thus, lipid-directed and tether-assisted Sar1 organization controls membrane constriction to regulate ER export. |
| doi_str_mv | 10.1083/jcb.201004132 |
| format | Article |
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Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). Sar1 activity was directed to liquid-disordered lipid phases. Thus, lipid-directed and tether-assisted Sar1 organization controls membrane constriction to regulate ER export.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.201004132</identifier><identifier>PMID: 20624903</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Animals ; Biological Transport - physiology ; Caco-2 Cells ; Cell Membrane - genetics ; Cell Membrane - metabolism ; Cellular biology ; COP-Coated Vesicles - genetics ; COP-Coated Vesicles - metabolism ; Dogs ; Endoplasmic Reticulum - genetics ; Endoplasmic Reticulum - metabolism ; Enzyme Activation - physiology ; Humans ; Lipids ; Membranes ; Monomeric GTP-Binding Proteins - genetics ; Monomeric GTP-Binding Proteins - metabolism ; Mutation ; Protein Multimerization - physiology ; Protein Structure, Secondary ; Proteins</subject><ispartof>The Journal of cell biology, 2010-07, Vol.190 (1), p.115-128</ispartof><rights>Copyright Rockefeller University Press Jul 12, 2010</rights><rights>2010 Long et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-a088468dbc51aed2f44770d3d2e150a0d3a3b6b44787818d3bd16954a071e4513</citedby><cites>FETCH-LOGICAL-c503t-a088468dbc51aed2f44770d3d2e150a0d3a3b6b44787818d3bd16954a071e4513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20624903$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Long, Kimberly R</creatorcontrib><creatorcontrib>Yamamoto, Yasunori</creatorcontrib><creatorcontrib>Baker, Adam L</creatorcontrib><creatorcontrib>Watkins, Simon C</creatorcontrib><creatorcontrib>Coyne, Carolyn B</creatorcontrib><creatorcontrib>Conway, James F</creatorcontrib><creatorcontrib>Aridor, Meir</creatorcontrib><title>Sar1 assembly regulates membrane constriction and ER export</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). Sar1 activity was directed to liquid-disordered lipid phases. Thus, lipid-directed and tether-assisted Sar1 organization controls membrane constriction to regulate ER export.</description><subject>Animals</subject><subject>Biological Transport - physiology</subject><subject>Caco-2 Cells</subject><subject>Cell Membrane - genetics</subject><subject>Cell Membrane - metabolism</subject><subject>Cellular biology</subject><subject>COP-Coated Vesicles - genetics</subject><subject>COP-Coated Vesicles - metabolism</subject><subject>Dogs</subject><subject>Endoplasmic Reticulum - genetics</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Enzyme Activation - physiology</subject><subject>Humans</subject><subject>Lipids</subject><subject>Membranes</subject><subject>Monomeric GTP-Binding Proteins - genetics</subject><subject>Monomeric GTP-Binding Proteins - metabolism</subject><subject>Mutation</subject><subject>Protein Multimerization - physiology</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctLxDAQxoMouj6OXrV48VSdSdIkRRBk8QULgo9zSNvs2qVt1qQV_e-N7LqopxlmfvPxDR8hhwhnCIqdz8vijAICcGR0g4ww45Aq5LBJRgAU0zyj2Q7ZDWEOEZKcbZMdCoLyHNiIXDwZj4kJwbZF85l4Oxsa09uQtHHgTWeT0nWh93XZ165LTFcl14-J_Vg43--Tralpgj1Y1T3ycnP9PL5LJw-39-OrSVpmwPrUgFJcqKooMzS2olPOpYSKVdRiBiZ2hhWiiFMlFaqKFRWKPOMGJFqeIdsjl0vdxVC0tipt13vT6IWvW-M_tTO1_rvp6lc9c--a5ohCyChwuhLw7m2woddtHUrbNPE_NwQtGcslB8YiefKPnLvBd_E7LSDPpeSCRihdQqV3IXg7XVtB0N-h6BiKXocS-aPf_tf0TwoROF4CU-O0mfk66JeneM8AlZCocvYFIMuP7w</recordid><startdate>20100712</startdate><enddate>20100712</enddate><creator>Long, Kimberly R</creator><creator>Yamamoto, Yasunori</creator><creator>Baker, Adam L</creator><creator>Watkins, Simon C</creator><creator>Coyne, Carolyn B</creator><creator>Conway, James F</creator><creator>Aridor, Meir</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100712</creationdate><title>Sar1 assembly regulates membrane constriction and ER export</title><author>Long, Kimberly R ; Yamamoto, Yasunori ; Baker, Adam L ; Watkins, Simon C ; Coyne, Carolyn B ; Conway, James F ; Aridor, Meir</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-a088468dbc51aed2f44770d3d2e150a0d3a3b6b44787818d3bd16954a071e4513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Biological Transport - physiology</topic><topic>Caco-2 Cells</topic><topic>Cell Membrane - genetics</topic><topic>Cell Membrane - metabolism</topic><topic>Cellular biology</topic><topic>COP-Coated Vesicles - genetics</topic><topic>COP-Coated Vesicles - metabolism</topic><topic>Dogs</topic><topic>Endoplasmic Reticulum - genetics</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Enzyme Activation - physiology</topic><topic>Humans</topic><topic>Lipids</topic><topic>Membranes</topic><topic>Monomeric GTP-Binding Proteins - genetics</topic><topic>Monomeric GTP-Binding Proteins - metabolism</topic><topic>Mutation</topic><topic>Protein Multimerization - physiology</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Long, Kimberly R</creatorcontrib><creatorcontrib>Yamamoto, Yasunori</creatorcontrib><creatorcontrib>Baker, Adam L</creatorcontrib><creatorcontrib>Watkins, Simon C</creatorcontrib><creatorcontrib>Coyne, Carolyn B</creatorcontrib><creatorcontrib>Conway, James F</creatorcontrib><creatorcontrib>Aridor, Meir</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Long, Kimberly R</au><au>Yamamoto, Yasunori</au><au>Baker, Adam L</au><au>Watkins, Simon C</au><au>Coyne, Carolyn B</au><au>Conway, James F</au><au>Aridor, Meir</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sar1 assembly regulates membrane constriction and ER export</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2010-07-12</date><risdate>2010</risdate><volume>190</volume><issue>1</issue><spage>115</spage><epage>128</epage><pages>115-128</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The guanosine triphosphatase Sar1 controls the assembly and fission of COPII vesicles. Sar1 utilizes an amphipathic N-terminal helix as a wedge that inserts into outer membrane leaflets to induce vesicle neck constriction and control fission. We hypothesize that Sar1 organizes on membranes to control constriction as observed with fission proteins like dynamin. Sar1 activation led to membrane-dependent oligomerization that transformed giant unilamellar vesicles into small vesicles connected through highly constricted necks. In contrast, membrane tension provided through membrane attachment led to organization of Sar1 in ordered scaffolds that formed rigid, uniformly nonconstricted lipid tubules to suggest that Sar1 organization regulates membrane constriction. Sar1 organization required conserved residues located on a unique C-terminal loop. Mutations in this loop did not affect Sar1 activation or COPII recruitment and enhanced membrane constriction, yet inhibited Sar1 organization and procollagen transport from the endoplasmic reticulum (ER). 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Biological Transport - physiology Caco-2 Cells Cell Membrane - genetics Cell Membrane - metabolism Cellular biology COP-Coated Vesicles - genetics COP-Coated Vesicles - metabolism Dogs Endoplasmic Reticulum - genetics Endoplasmic Reticulum - metabolism Enzyme Activation - physiology Humans Lipids Membranes Monomeric GTP-Binding Proteins - genetics Monomeric GTP-Binding Proteins - metabolism Mutation Protein Multimerization - physiology Protein Structure, Secondary Proteins |
| title | Sar1 assembly regulates membrane constriction and ER export |
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