Mutual Control of Membrane Fission and Fusion Proteins
Membrane fusion and fission are antagonistic reactions controlled by different proteins. Dynamins promote membrane fission by GTP-driven changes of conformation and polymerization state, while SNAREs fuse membranes by forming complexes between t- and v-SNAREs from apposed vesicles. Here, we describe...
Gespeichert in:
Veröffentlicht in: | Cell 2004-11, Vol.119 (5), p.667-678 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 678 |
---|---|
container_issue | 5 |
container_start_page | 667 |
container_title | Cell |
container_volume | 119 |
creator | Peters, Christopher Baars, Tonie L. Bühler, Susanne Mayer, Andreas |
description | Membrane fusion and fission are antagonistic reactions controlled by different proteins. Dynamins promote membrane fission by GTP-driven changes of conformation and polymerization state, while SNAREs fuse membranes by forming complexes between t- and v-SNAREs from apposed vesicles. Here, we describe a role of the dynamin-like GTPase Vps1p in fusion of yeast vacuoles. Vps1p forms polymers that couple several t-SNAREs together. At the onset of fusion, the SNARE-activating ATPase Sec18p/NSF and the t-SNARE depolymerize Vps1p and release it from the membrane. This activity is independent of the SNARE coactivator Sec17p/α-SNAP and of the v-SNARE. Vps1p release liberates the t-SNAREs for initiating fusion and at the same time disrupts fission activity. We propose that reciprocal control between fusion and fission components exists, which may prevent futile cycles of fission and fusion. |
doi_str_mv | 10.1016/j.cell.2004.11.023 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67092382</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0092867404010918</els_id><sourcerecordid>17793902</sourcerecordid><originalsourceid>FETCH-LOGICAL-c427t-520ff7bfbbf843b1261ff1980829e2f24af4ab7bcc06f433a0b653a5e3b447733</originalsourceid><addsrcrecordid>eNqFkD9PwzAUxC0EoqXwBRhQJraE5z-JE4kFVS0gtYIBZst2bMlVEhc7QeLbk9BKbDDdG353encIXWPIMODibpdp0zQZAWAZxhkQeoLmGCqeMszJKZoDVCQtC85m6CLGHQCUeZ6foxkeBQgr56jYDv0gm2Tpuz74JvE22ZpWBdmZZO1idL5LZFcn6-HnfA2-N66Ll-jMyiaaq6Mu0Pt69bZ8Sjcvj8_Lh02qGeF9mhOwliurlC0ZVZgU2FpclVCSyhBLmLRMKq60hsIySiWoIqcyN1QxxjmlC3R7yN0H_zGY2IvWxan1-J8foij4WJGW5F8Qc17RCiaQHEAdfIzBWLEPrpXhS2AQ06xiJyafmGYVGIvRM5pujumDak39aznuOAL3B8CMY3w6E0TUznTa1C4Y3Yvau7_yvwEEJoeG</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17793902</pqid></control><display><type>article</type><title>Mutual Control of Membrane Fission and Fusion Proteins</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Peters, Christopher ; Baars, Tonie L. ; Bühler, Susanne ; Mayer, Andreas</creator><creatorcontrib>Peters, Christopher ; Baars, Tonie L. ; Bühler, Susanne ; Mayer, Andreas</creatorcontrib><description>Membrane fusion and fission are antagonistic reactions controlled by different proteins. Dynamins promote membrane fission by GTP-driven changes of conformation and polymerization state, while SNAREs fuse membranes by forming complexes between t- and v-SNAREs from apposed vesicles. Here, we describe a role of the dynamin-like GTPase Vps1p in fusion of yeast vacuoles. Vps1p forms polymers that couple several t-SNAREs together. At the onset of fusion, the SNARE-activating ATPase Sec18p/NSF and the t-SNARE depolymerize Vps1p and release it from the membrane. This activity is independent of the SNARE coactivator Sec17p/α-SNAP and of the v-SNARE. Vps1p release liberates the t-SNAREs for initiating fusion and at the same time disrupts fission activity. We propose that reciprocal control between fusion and fission components exists, which may prevent futile cycles of fission and fusion.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2004.11.023</identifier><identifier>PMID: 15550248</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphatases - metabolism ; Carrier Proteins - metabolism ; Dynamins - genetics ; Dynamins - metabolism ; GTP-Binding Proteins - metabolism ; Intracellular Membranes - metabolism ; Membrane Fusion - genetics ; Membrane Proteins - metabolism ; Models, Biological ; Organelles - metabolism ; Protein Transport - physiology ; Qa-SNARE Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - metabolism ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; Vacuoles - metabolism ; Vesicular Transport Proteins - metabolism</subject><ispartof>Cell, 2004-11, Vol.119 (5), p.667-678</ispartof><rights>2004 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-520ff7bfbbf843b1261ff1980829e2f24af4ab7bcc06f433a0b653a5e3b447733</citedby><cites>FETCH-LOGICAL-c427t-520ff7bfbbf843b1261ff1980829e2f24af4ab7bcc06f433a0b653a5e3b447733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cell.2004.11.023$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15550248$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Peters, Christopher</creatorcontrib><creatorcontrib>Baars, Tonie L.</creatorcontrib><creatorcontrib>Bühler, Susanne</creatorcontrib><creatorcontrib>Mayer, Andreas</creatorcontrib><title>Mutual Control of Membrane Fission and Fusion Proteins</title><title>Cell</title><addtitle>Cell</addtitle><description>Membrane fusion and fission are antagonistic reactions controlled by different proteins. Dynamins promote membrane fission by GTP-driven changes of conformation and polymerization state, while SNAREs fuse membranes by forming complexes between t- and v-SNAREs from apposed vesicles. Here, we describe a role of the dynamin-like GTPase Vps1p in fusion of yeast vacuoles. Vps1p forms polymers that couple several t-SNAREs together. At the onset of fusion, the SNARE-activating ATPase Sec18p/NSF and the t-SNARE depolymerize Vps1p and release it from the membrane. This activity is independent of the SNARE coactivator Sec17p/α-SNAP and of the v-SNARE. Vps1p release liberates the t-SNAREs for initiating fusion and at the same time disrupts fission activity. We propose that reciprocal control between fusion and fission components exists, which may prevent futile cycles of fission and fusion.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Carrier Proteins - metabolism</subject><subject>Dynamins - genetics</subject><subject>Dynamins - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Intracellular Membranes - metabolism</subject><subject>Membrane Fusion - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Organelles - metabolism</subject><subject>Protein Transport - physiology</subject><subject>Qa-SNARE Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>SNARE Proteins</subject><subject>Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins</subject><subject>Vacuoles - metabolism</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD9PwzAUxC0EoqXwBRhQJraE5z-JE4kFVS0gtYIBZst2bMlVEhc7QeLbk9BKbDDdG353encIXWPIMODibpdp0zQZAWAZxhkQeoLmGCqeMszJKZoDVCQtC85m6CLGHQCUeZ6foxkeBQgr56jYDv0gm2Tpuz74JvE22ZpWBdmZZO1idL5LZFcn6-HnfA2-N66Ll-jMyiaaq6Mu0Pt69bZ8Sjcvj8_Lh02qGeF9mhOwliurlC0ZVZgU2FpclVCSyhBLmLRMKq60hsIySiWoIqcyN1QxxjmlC3R7yN0H_zGY2IvWxan1-J8foij4WJGW5F8Qc17RCiaQHEAdfIzBWLEPrpXhS2AQ06xiJyafmGYVGIvRM5pujumDak39aznuOAL3B8CMY3w6E0TUznTa1C4Y3Yvau7_yvwEEJoeG</recordid><startdate>20041124</startdate><enddate>20041124</enddate><creator>Peters, Christopher</creator><creator>Baars, Tonie L.</creator><creator>Bühler, Susanne</creator><creator>Mayer, Andreas</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>20041124</creationdate><title>Mutual Control of Membrane Fission and Fusion Proteins</title><author>Peters, Christopher ; Baars, Tonie L. ; Bühler, Susanne ; Mayer, Andreas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-520ff7bfbbf843b1261ff1980829e2f24af4ab7bcc06f433a0b653a5e3b447733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>Dynamins - genetics</topic><topic>Dynamins - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Intracellular Membranes - metabolism</topic><topic>Membrane Fusion - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Models, Biological</topic><topic>Organelles - metabolism</topic><topic>Protein Transport - physiology</topic><topic>Qa-SNARE Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>SNARE Proteins</topic><topic>Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins</topic><topic>Vacuoles - metabolism</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Peters, Christopher</creatorcontrib><creatorcontrib>Baars, Tonie L.</creatorcontrib><creatorcontrib>Bühler, Susanne</creatorcontrib><creatorcontrib>Mayer, Andreas</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Peters, Christopher</au><au>Baars, Tonie L.</au><au>Bühler, Susanne</au><au>Mayer, Andreas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutual Control of Membrane Fission and Fusion Proteins</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2004-11-24</date><risdate>2004</risdate><volume>119</volume><issue>5</issue><spage>667</spage><epage>678</epage><pages>667-678</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Membrane fusion and fission are antagonistic reactions controlled by different proteins. Dynamins promote membrane fission by GTP-driven changes of conformation and polymerization state, while SNAREs fuse membranes by forming complexes between t- and v-SNAREs from apposed vesicles. Here, we describe a role of the dynamin-like GTPase Vps1p in fusion of yeast vacuoles. Vps1p forms polymers that couple several t-SNAREs together. At the onset of fusion, the SNARE-activating ATPase Sec18p/NSF and the t-SNARE depolymerize Vps1p and release it from the membrane. This activity is independent of the SNARE coactivator Sec17p/α-SNAP and of the v-SNARE. Vps1p release liberates the t-SNAREs for initiating fusion and at the same time disrupts fission activity. We propose that reciprocal control between fusion and fission components exists, which may prevent futile cycles of fission and fusion.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15550248</pmid><doi>10.1016/j.cell.2004.11.023</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0092-8674 |
ispartof | Cell, 2004-11, Vol.119 (5), p.667-678 |
issn | 0092-8674 1097-4172 |
language | eng |
recordid | cdi_proquest_miscellaneous_67092382 |
source | MEDLINE; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present) |
subjects | Adenosine Triphosphatases - metabolism Carrier Proteins - metabolism Dynamins - genetics Dynamins - metabolism GTP-Binding Proteins - metabolism Intracellular Membranes - metabolism Membrane Fusion - genetics Membrane Proteins - metabolism Models, Biological Organelles - metabolism Protein Transport - physiology Qa-SNARE Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - metabolism SNARE Proteins Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Vacuoles - metabolism Vesicular Transport Proteins - metabolism |
title | Mutual Control of Membrane Fission and Fusion Proteins |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T16%3A52%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mutual%20Control%20of%20Membrane%20Fission%20and%20Fusion%20Proteins&rft.jtitle=Cell&rft.au=Peters,%20Christopher&rft.date=2004-11-24&rft.volume=119&rft.issue=5&rft.spage=667&rft.epage=678&rft.pages=667-678&rft.issn=0092-8674&rft.eissn=1097-4172&rft_id=info:doi/10.1016/j.cell.2004.11.023&rft_dat=%3Cproquest_cross%3E17793902%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17793902&rft_id=info:pmid/15550248&rft_els_id=S0092867404010918&rfr_iscdi=true |