The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport: e1004644
Axonal transport of synaptic vesicles (SVs) is a KIF1A/UNC-104 mediated process critical for synapse development and maintenance yet little is known of how SV transport is regulated. Using C. elegans as an in vivo model, we identified SAM-4 as a novel conserved vesicular component regulating SV tran...
Gespeichert in:
| Veröffentlicht in: | PLoS genetics 2014-10, Vol.10 (10) |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 10 |
| container_start_page | |
| container_title | PLoS genetics |
| container_volume | 10 |
| creator | Zheng, Qun Ahlawat, Shikha Schaefer, Anneliese Mahoney, Tim Koushika, Sandhya P Nonet, Michael L |
| description | Axonal transport of synaptic vesicles (SVs) is a KIF1A/UNC-104 mediated process critical for synapse development and maintenance yet little is known of how SV transport is regulated. Using C. elegans as an in vivo model, we identified SAM-4 as a novel conserved vesicular component regulating SV transport. Processivity, but not velocity, of SV transport was reduced in sam-4 mutants. sam-4 displayed strong genetic interactions with mutations in the cargo binding but not the motor domain of unc-104. Gain-of-function mutations in the unc-104 motor domain, identified in this study, suppress the sam-4 defects by increasing processivity of the SV transport. Genetic analyses suggest that SAM-4, SYD-2/liprin-α and the KIF1A/UNC-104 motor function in the same pathway to regulate SV transport. Our data support a model in which the SV protein SAM-4 regulates the processivity of SV transport. |
| doi_str_mv | 10.1371/journal.pgen.1004644 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_1691281384</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3702547221</sourcerecordid><originalsourceid>FETCH-LOGICAL-p614-57d413e6a461025018dfb8e1dd8b9c389c5983737bf08f04d3c802a043e09c543</originalsourceid><addsrcrecordid>eNpdkD9PwzAUxC0EEqXwDRgssbAk-OXZiT1WFf-kIlAbsVau89KmCkmIHaR-eygUBqY76X53wzF2CSIGzOBm2w59Y-u4W1MTgxAylfKIjUApjDIp5PGvRyNO2Zn3WyFQaZON2DzfEH8lX7ma-EvfBqoavpg8RZLPaT3UNpDnYfOdOfK--qjCjrclX-wa24XK_ZXz3ja-a_twzk5KW3u6OOiY5Xe3-fQhmj3fP04ns6hLQUYqKyQgpVamIBIlQBflShMUhV4Zh9o4ZTRmmK1KoUshC3RaJFZIJPGVSRyz65_Zrm_fB_Jh-VZ5R3VtG2oHv4TUQKIB9R69-oceHttTWkFiMoX4CeZnYO0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1685129753</pqid></control><display><type>article</type><title>The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport: e1004644</title><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Public Library of Science (PLoS)</source><source>PubMed Central</source><creator>Zheng, Qun ; Ahlawat, Shikha ; Schaefer, Anneliese ; Mahoney, Tim ; Koushika, Sandhya P ; Nonet, Michael L</creator><creatorcontrib>Zheng, Qun ; Ahlawat, Shikha ; Schaefer, Anneliese ; Mahoney, Tim ; Koushika, Sandhya P ; Nonet, Michael L</creatorcontrib><description>Axonal transport of synaptic vesicles (SVs) is a KIF1A/UNC-104 mediated process critical for synapse development and maintenance yet little is known of how SV transport is regulated. Using C. elegans as an in vivo model, we identified SAM-4 as a novel conserved vesicular component regulating SV transport. Processivity, but not velocity, of SV transport was reduced in sam-4 mutants. sam-4 displayed strong genetic interactions with mutations in the cargo binding but not the motor domain of unc-104. Gain-of-function mutations in the unc-104 motor domain, identified in this study, suppress the sam-4 defects by increasing processivity of the SV transport. Genetic analyses suggest that SAM-4, SYD-2/liprin-α and the KIF1A/UNC-104 motor function in the same pathway to regulate SV transport. Our data support a model in which the SV protein SAM-4 regulates the processivity of SV transport.</description><identifier>ISSN: 1553-7390</identifier><identifier>EISSN: 1553-7404</identifier><identifier>DOI: 10.1371/journal.pgen.1004644</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Mutation ; Nematodes ; Neurons ; Paralysis ; Phosphorylation ; Proteins</subject><ispartof>PLoS genetics, 2014-10, Vol.10 (10)</ispartof><rights>2014 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Zheng Q, Ahlawat S, Schaefer A, Mahoney T, Koushika SP, Nonet ML (2014) The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport. PLoS Genet 10(10): e1004644. doi:10.1371/journal.pgen.1004644</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,861,27905,27906</link.rule.ids></links><search><creatorcontrib>Zheng, Qun</creatorcontrib><creatorcontrib>Ahlawat, Shikha</creatorcontrib><creatorcontrib>Schaefer, Anneliese</creatorcontrib><creatorcontrib>Mahoney, Tim</creatorcontrib><creatorcontrib>Koushika, Sandhya P</creatorcontrib><creatorcontrib>Nonet, Michael L</creatorcontrib><title>The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport: e1004644</title><title>PLoS genetics</title><description>Axonal transport of synaptic vesicles (SVs) is a KIF1A/UNC-104 mediated process critical for synapse development and maintenance yet little is known of how SV transport is regulated. Using C. elegans as an in vivo model, we identified SAM-4 as a novel conserved vesicular component regulating SV transport. Processivity, but not velocity, of SV transport was reduced in sam-4 mutants. sam-4 displayed strong genetic interactions with mutations in the cargo binding but not the motor domain of unc-104. Gain-of-function mutations in the unc-104 motor domain, identified in this study, suppress the sam-4 defects by increasing processivity of the SV transport. Genetic analyses suggest that SAM-4, SYD-2/liprin-α and the KIF1A/UNC-104 motor function in the same pathway to regulate SV transport. Our data support a model in which the SV protein SAM-4 regulates the processivity of SV transport.</description><subject>Mutation</subject><subject>Nematodes</subject><subject>Neurons</subject><subject>Paralysis</subject><subject>Phosphorylation</subject><subject>Proteins</subject><issn>1553-7390</issn><issn>1553-7404</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkD9PwzAUxC0EEqXwDRgssbAk-OXZiT1WFf-kIlAbsVau89KmCkmIHaR-eygUBqY76X53wzF2CSIGzOBm2w59Y-u4W1MTgxAylfKIjUApjDIp5PGvRyNO2Zn3WyFQaZON2DzfEH8lX7ma-EvfBqoavpg8RZLPaT3UNpDnYfOdOfK--qjCjrclX-wa24XK_ZXz3ja-a_twzk5KW3u6OOiY5Xe3-fQhmj3fP04ns6hLQUYqKyQgpVamIBIlQBflShMUhV4Zh9o4ZTRmmK1KoUshC3RaJFZIJPGVSRyz65_Zrm_fB_Jh-VZ5R3VtG2oHv4TUQKIB9R69-oceHttTWkFiMoX4CeZnYO0</recordid><startdate>20141001</startdate><enddate>20141001</enddate><creator>Zheng, Qun</creator><creator>Ahlawat, Shikha</creator><creator>Schaefer, Anneliese</creator><creator>Mahoney, Tim</creator><creator>Koushika, Sandhya P</creator><creator>Nonet, Michael L</creator><general>Public Library of Science</general><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope></search><sort><creationdate>20141001</creationdate><title>The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport</title><author>Zheng, Qun ; Ahlawat, Shikha ; Schaefer, Anneliese ; Mahoney, Tim ; Koushika, Sandhya P ; Nonet, Michael L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p614-57d413e6a461025018dfb8e1dd8b9c389c5983737bf08f04d3c802a043e09c543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Mutation</topic><topic>Nematodes</topic><topic>Neurons</topic><topic>Paralysis</topic><topic>Phosphorylation</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zheng, Qun</creatorcontrib><creatorcontrib>Ahlawat, Shikha</creatorcontrib><creatorcontrib>Schaefer, Anneliese</creatorcontrib><creatorcontrib>Mahoney, Tim</creatorcontrib><creatorcontrib>Koushika, Sandhya P</creatorcontrib><creatorcontrib>Nonet, Michael L</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><jtitle>PLoS genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zheng, Qun</au><au>Ahlawat, Shikha</au><au>Schaefer, Anneliese</au><au>Mahoney, Tim</au><au>Koushika, Sandhya P</au><au>Nonet, Michael L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport: e1004644</atitle><jtitle>PLoS genetics</jtitle><date>2014-10-01</date><risdate>2014</risdate><volume>10</volume><issue>10</issue><issn>1553-7390</issn><eissn>1553-7404</eissn><abstract>Axonal transport of synaptic vesicles (SVs) is a KIF1A/UNC-104 mediated process critical for synapse development and maintenance yet little is known of how SV transport is regulated. Using C. elegans as an in vivo model, we identified SAM-4 as a novel conserved vesicular component regulating SV transport. Processivity, but not velocity, of SV transport was reduced in sam-4 mutants. sam-4 displayed strong genetic interactions with mutations in the cargo binding but not the motor domain of unc-104. Gain-of-function mutations in the unc-104 motor domain, identified in this study, suppress the sam-4 defects by increasing processivity of the SV transport. Genetic analyses suggest that SAM-4, SYD-2/liprin-α and the KIF1A/UNC-104 motor function in the same pathway to regulate SV transport. Our data support a model in which the SV protein SAM-4 regulates the processivity of SV transport.</abstract><cop>San Francisco</cop><pub>Public Library of Science</pub><doi>10.1371/journal.pgen.1004644</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1553-7390 |
| ispartof | PLoS genetics, 2014-10, Vol.10 (10) |
| issn | 1553-7390 1553-7404 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1691281384 |
| source | DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central |
| subjects | Mutation Nematodes Neurons Paralysis Phosphorylation Proteins |
| title | The Vesicle Protein SAM-4 Regulates the Processivity of Synaptic Vesicle Transport: e1004644 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T03%3A13%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Vesicle%20Protein%20SAM-4%20Regulates%20the%20Processivity%20of%20Synaptic%20Vesicle%20Transport:%20e1004644&rft.jtitle=PLoS%20genetics&rft.au=Zheng,%20Qun&rft.date=2014-10-01&rft.volume=10&rft.issue=10&rft.issn=1553-7390&rft.eissn=1553-7404&rft_id=info:doi/10.1371/journal.pgen.1004644&rft_dat=%3Cproquest%3E3702547221%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1685129753&rft_id=info:pmid/&rfr_iscdi=true |