Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex
Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to tra...
Gespeichert in:
| Veröffentlicht in: | Developmental cell 2011-12, Vol.21 (6), p.1156-1170 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1170 |
|---|---|
| container_issue | 6 |
| container_start_page | 1156 |
| container_title | Developmental cell |
| container_volume | 21 |
| creator | Jin, Yui Sultana, Azmiri Gandhi, Pallavi Franklin, Edward Hamamoto, Susan Khan, Amir R. Munson, Mary Schekman, Randy Weisman, Lois S. |
| description | Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.
[Display omitted]
► Three Rab GTPases (Ypt31/32 and Sec4) associate with the same region of myosin V (Myo2) ► The exocyst subunit Sec15 interacts with a distinct portion of Myo2 ► These interactions are essential for secretory vesicle transport in budding yeast ► Mammalian myosin Va also interacts with the exocyst complex |
| doi_str_mv | 10.1016/j.devcel.2011.10.009 |
| format | Article |
| fullrecord | <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3241923</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1534580711004564</els_id><sourcerecordid>22172676</sourcerecordid><originalsourceid>FETCH-LOGICAL-c492t-a2720fa5a8d16f5d1da0118389bde1ad4c1b12925c840111ebcd126c297bdbd23</originalsourceid><addsrcrecordid>eNp9kE1vEzEQhi0EoqXwDxDyheOmHu96Py5IKCqlUiuqEnq1Zu1Z4mizjmw3NP8eRyn9uHCa0cz7vvY8jH0EMQMB9elqZmlraJxJAZBHMyG6V-wY2qYtQCl4nXtVVoVqRXPE3sW4EtkGrXjLjqSERtZNfcyWVzsf3cRv-SLgFDc-pMh_kgmUfNjxW4rOjBT51iFHfoM9P19cYyQ-x2jQEsfJ8ospUUCTnJ_4H5eWPC2Jn917s4uJz_16M9L9e_ZmwDHSh4d6wn59O1vMvxeXP84v5l8vC1N1MhUoGykGVNhaqAdlwWI-ry3brrcEaCsDPchOKtNWeQHUGwuyNrJrettbWZ6wL4fczV2_JmtoSgFHvQlujWGnPTr9cjO5pf7tt7qUFXSyzAHVIcAEH2Og4dELQu_J65U-kNd78vtpJp9tn56_-2j6hzoLPj8I9uTGIeM2Lj7pVAmlVM3TAZQpbR0FHY2jyZB1gUzS1rv__-QvfDqlew</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Jin, Yui ; Sultana, Azmiri ; Gandhi, Pallavi ; Franklin, Edward ; Hamamoto, Susan ; Khan, Amir R. ; Munson, Mary ; Schekman, Randy ; Weisman, Lois S.</creator><creatorcontrib>Jin, Yui ; Sultana, Azmiri ; Gandhi, Pallavi ; Franklin, Edward ; Hamamoto, Susan ; Khan, Amir R. ; Munson, Mary ; Schekman, Randy ; Weisman, Lois S.</creatorcontrib><description>Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.
[Display omitted]
► Three Rab GTPases (Ypt31/32 and Sec4) associate with the same region of myosin V (Myo2) ► The exocyst subunit Sec15 interacts with a distinct portion of Myo2 ► These interactions are essential for secretory vesicle transport in budding yeast ► Mammalian myosin Va also interacts with the exocyst complex</description><identifier>ISSN: 1534-5807</identifier><identifier>EISSN: 1878-1551</identifier><identifier>DOI: 10.1016/j.devcel.2011.10.009</identifier><identifier>PMID: 22172676</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>Amino Acid Substitution ; Binding Sites ; Biological and medical sciences ; Cell differentiation, maturation, development, hematopoiesis ; Cell physiology ; Exocytosis ; Fundamental and applied biological sciences. Psychology ; Membrane Fusion ; Models, Molecular ; Molecular and cellular biology ; Molecular Motor Proteins - metabolism ; Mutagenesis, Site-Directed ; Myosin Heavy Chains - chemistry ; Myosin Heavy Chains - genetics ; Myosin Heavy Chains - metabolism ; Myosin Type V - chemistry ; Myosin Type V - genetics ; Myosin Type V - metabolism ; Protein Interaction Domains and Motifs ; rab GTP-Binding Proteins - genetics ; rab GTP-Binding Proteins - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Secretory Vesicles - metabolism ; Signal Transduction ; Vesicular Transport Proteins - chemistry ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism</subject><ispartof>Developmental cell, 2011-12, Vol.21 (6), p.1156-1170</ispartof><rights>2011 Elsevier Inc.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><rights>2011 Elsevier Inc. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-a2720fa5a8d16f5d1da0118389bde1ad4c1b12925c840111ebcd126c297bdbd23</citedby><cites>FETCH-LOGICAL-c492t-a2720fa5a8d16f5d1da0118389bde1ad4c1b12925c840111ebcd126c297bdbd23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1534580711004564$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25313257$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22172676$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jin, Yui</creatorcontrib><creatorcontrib>Sultana, Azmiri</creatorcontrib><creatorcontrib>Gandhi, Pallavi</creatorcontrib><creatorcontrib>Franklin, Edward</creatorcontrib><creatorcontrib>Hamamoto, Susan</creatorcontrib><creatorcontrib>Khan, Amir R.</creatorcontrib><creatorcontrib>Munson, Mary</creatorcontrib><creatorcontrib>Schekman, Randy</creatorcontrib><creatorcontrib>Weisman, Lois S.</creatorcontrib><title>Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex</title><title>Developmental cell</title><addtitle>Dev Cell</addtitle><description>Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.
[Display omitted]
► Three Rab GTPases (Ypt31/32 and Sec4) associate with the same region of myosin V (Myo2) ► The exocyst subunit Sec15 interacts with a distinct portion of Myo2 ► These interactions are essential for secretory vesicle transport in budding yeast ► Mammalian myosin Va also interacts with the exocyst complex</description><subject>Amino Acid Substitution</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cell differentiation, maturation, development, hematopoiesis</subject><subject>Cell physiology</subject><subject>Exocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Membrane Fusion</subject><subject>Models, Molecular</subject><subject>Molecular and cellular biology</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Mutagenesis, Site-Directed</subject><subject>Myosin Heavy Chains - chemistry</subject><subject>Myosin Heavy Chains - genetics</subject><subject>Myosin Heavy Chains - metabolism</subject><subject>Myosin Type V - chemistry</subject><subject>Myosin Type V - genetics</subject><subject>Myosin Type V - metabolism</subject><subject>Protein Interaction Domains and Motifs</subject><subject>rab GTP-Binding Proteins - genetics</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Secretory Vesicles - metabolism</subject><subject>Signal Transduction</subject><subject>Vesicular Transport Proteins - chemistry</subject><subject>Vesicular Transport Proteins - genetics</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>1534-5807</issn><issn>1878-1551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1vEzEQhi0EoqXwDxDyheOmHu96Py5IKCqlUiuqEnq1Zu1Z4mizjmw3NP8eRyn9uHCa0cz7vvY8jH0EMQMB9elqZmlraJxJAZBHMyG6V-wY2qYtQCl4nXtVVoVqRXPE3sW4EtkGrXjLjqSERtZNfcyWVzsf3cRv-SLgFDc-pMh_kgmUfNjxW4rOjBT51iFHfoM9P19cYyQ-x2jQEsfJ8ospUUCTnJ_4H5eWPC2Jn917s4uJz_16M9L9e_ZmwDHSh4d6wn59O1vMvxeXP84v5l8vC1N1MhUoGykGVNhaqAdlwWI-ry3brrcEaCsDPchOKtNWeQHUGwuyNrJrettbWZ6wL4fczV2_JmtoSgFHvQlujWGnPTr9cjO5pf7tt7qUFXSyzAHVIcAEH2Og4dELQu_J65U-kNd78vtpJp9tn56_-2j6hzoLPj8I9uTGIeM2Lj7pVAmlVM3TAZQpbR0FHY2jyZB1gUzS1rv__-QvfDqlew</recordid><startdate>20111213</startdate><enddate>20111213</enddate><creator>Jin, Yui</creator><creator>Sultana, Azmiri</creator><creator>Gandhi, Pallavi</creator><creator>Franklin, Edward</creator><creator>Hamamoto, Susan</creator><creator>Khan, Amir R.</creator><creator>Munson, Mary</creator><creator>Schekman, Randy</creator><creator>Weisman, Lois S.</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>6I.</scope><scope>AAFTH</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>5PM</scope></search><sort><creationdate>20111213</creationdate><title>Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex</title><author>Jin, Yui ; Sultana, Azmiri ; Gandhi, Pallavi ; Franklin, Edward ; Hamamoto, Susan ; Khan, Amir R. ; Munson, Mary ; Schekman, Randy ; Weisman, Lois S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-a2720fa5a8d16f5d1da0118389bde1ad4c1b12925c840111ebcd126c297bdbd23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Substitution</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cell differentiation, maturation, development, hematopoiesis</topic><topic>Cell physiology</topic><topic>Exocytosis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Membrane Fusion</topic><topic>Models, Molecular</topic><topic>Molecular and cellular biology</topic><topic>Molecular Motor Proteins - metabolism</topic><topic>Mutagenesis, Site-Directed</topic><topic>Myosin Heavy Chains - chemistry</topic><topic>Myosin Heavy Chains - genetics</topic><topic>Myosin Heavy Chains - metabolism</topic><topic>Myosin Type V - chemistry</topic><topic>Myosin Type V - genetics</topic><topic>Myosin Type V - metabolism</topic><topic>Protein Interaction Domains and Motifs</topic><topic>rab GTP-Binding Proteins - genetics</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Secretory Vesicles - metabolism</topic><topic>Signal Transduction</topic><topic>Vesicular Transport Proteins - chemistry</topic><topic>Vesicular Transport Proteins - genetics</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jin, Yui</creatorcontrib><creatorcontrib>Sultana, Azmiri</creatorcontrib><creatorcontrib>Gandhi, Pallavi</creatorcontrib><creatorcontrib>Franklin, Edward</creatorcontrib><creatorcontrib>Hamamoto, Susan</creatorcontrib><creatorcontrib>Khan, Amir R.</creatorcontrib><creatorcontrib>Munson, Mary</creatorcontrib><creatorcontrib>Schekman, Randy</creatorcontrib><creatorcontrib>Weisman, Lois S.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Developmental cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jin, Yui</au><au>Sultana, Azmiri</au><au>Gandhi, Pallavi</au><au>Franklin, Edward</au><au>Hamamoto, Susan</au><au>Khan, Amir R.</au><au>Munson, Mary</au><au>Schekman, Randy</au><au>Weisman, Lois S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex</atitle><jtitle>Developmental cell</jtitle><addtitle>Dev Cell</addtitle><date>2011-12-13</date><risdate>2011</risdate><volume>21</volume><issue>6</issue><spage>1156</spage><epage>1170</epage><pages>1156-1170</pages><issn>1534-5807</issn><eissn>1878-1551</eissn><abstract>Vesicle transport requires four steps: vesicle formation, movement, tethering, and fusion. In yeast, two Rab GTPases, Ypt31/32, are required for post-Golgi vesicle formation. A third Rab GTPase, Sec4, and the exocyst act in tethering and fusion of these vesicles. Vesicle production is coupled to transport via direct interaction between Ypt31/32 and the yeast myosin V, Myo2. Here we show that Myo2 interacts directly with Sec4 and the exocyst subunit Sec15. Disruption of these interactions results in compromised growth and the accumulation of secretory vesicles. We identified the Sec15-binding region on Myo2 and also identified residues on Sec15 required for interaction with Myo2. That Myo2 interacts with Sec15 uncovers additional roles for the exocyst as an adaptor for molecular motors and implies similar roles for structurally related tethering complexes. Moreover, these studies predict that for many pathways, molecular motors attach to vesicles prior to their formation and remain attached until fusion.
[Display omitted]
► Three Rab GTPases (Ypt31/32 and Sec4) associate with the same region of myosin V (Myo2) ► The exocyst subunit Sec15 interacts with a distinct portion of Myo2 ► These interactions are essential for secretory vesicle transport in budding yeast ► Mammalian myosin Va also interacts with the exocyst complex</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>22172676</pmid><doi>10.1016/j.devcel.2011.10.009</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1534-5807 |
| ispartof | Developmental cell, 2011-12, Vol.21 (6), p.1156-1170 |
| issn | 1534-5807 1878-1551 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3241923 |
| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Substitution Binding Sites Biological and medical sciences Cell differentiation, maturation, development, hematopoiesis Cell physiology Exocytosis Fundamental and applied biological sciences. Psychology Membrane Fusion Models, Molecular Molecular and cellular biology Molecular Motor Proteins - metabolism Mutagenesis, Site-Directed Myosin Heavy Chains - chemistry Myosin Heavy Chains - genetics Myosin Heavy Chains - metabolism Myosin Type V - chemistry Myosin Type V - genetics Myosin Type V - metabolism Protein Interaction Domains and Motifs rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Secretory Vesicles - metabolism Signal Transduction Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism |
| title | Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T12%3A07%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Myosin%20V%20Transports%20Secretory%20Vesicles%20via%20a%20Rab%20GTPase%20Cascade%20and%20Interaction%20with%20the%20Exocyst%20Complex&rft.jtitle=Developmental%20cell&rft.au=Jin,%20Yui&rft.date=2011-12-13&rft.volume=21&rft.issue=6&rft.spage=1156&rft.epage=1170&rft.pages=1156-1170&rft.issn=1534-5807&rft.eissn=1878-1551&rft_id=info:doi/10.1016/j.devcel.2011.10.009&rft_dat=%3Cpubmed_cross%3E22172676%3C/pubmed_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/22172676&rft_els_id=S1534580711004564&rfr_iscdi=true |