Rabphilin Potentiates Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Function Independently of rab3
Rabphilin, a putative rab effector, interacts specifically with the GTP-bound form of the synaptic vesicle-associated protein rab3a. In this study, we define in vivo functions for rabphilin through the characterization of mutants that disrupt the Caenorhabditis elegans rabphilin homolog. The mutants...
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| Veröffentlicht in: | The Journal of neuroscience 2001-12, Vol.21 (23), p.9255-9264 |
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| creator | Staunton, Jane Ganetzky, Barry Nonet, Michael L |
| description | Rabphilin, a putative rab effector, interacts specifically with the GTP-bound form of the synaptic vesicle-associated protein rab3a. In this study, we define in vivo functions for rabphilin through the characterization of mutants that disrupt the Caenorhabditis elegans rabphilin homolog. The mutants do not display the general synaptic defects associated with rab3 lesions, as assayed at the pharmacological, physiological, and ultrastructural level. However, rabphilin mutants exhibit severe lethargy in the absence of mechanical stimulation. Furthermore, rabphilin mutations display strong synergistic interactions with hypomorphic lesions in the syntaxin, synaptosomal-associated protein of 25 kDa, and synaptobrevin soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) genes; double mutants were nonresponsive to mechanical stimulation. These synergistic interactions were independent of rab3 function and were not observed in rab3-SNARE double mutants. Our data reveal rab3-independent functions for rabphilin in the potentiation of SNARE function. |
| doi_str_mv | 10.1523/JNEUROSCI.21-23-09255.2001 |
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In this study, we define in vivo functions for rabphilin through the characterization of mutants that disrupt the Caenorhabditis elegans rabphilin homolog. The mutants do not display the general synaptic defects associated with rab3 lesions, as assayed at the pharmacological, physiological, and ultrastructural level. However, rabphilin mutants exhibit severe lethargy in the absence of mechanical stimulation. Furthermore, rabphilin mutations display strong synergistic interactions with hypomorphic lesions in the syntaxin, synaptosomal-associated protein of 25 kDa, and synaptobrevin soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) genes; double mutants were nonresponsive to mechanical stimulation. These synergistic interactions were independent of rab3 function and were not observed in rab3-SNARE double mutants. Our data reveal rab3-independent functions for rabphilin in the potentiation of SNARE function.</description><identifier>ISSN: 0270-6474</identifier><identifier>ISSN: 1529-2401</identifier><identifier>EISSN: 1529-2401</identifier><identifier>DOI: 10.1523/JNEUROSCI.21-23-09255.2001</identifier><identifier>PMID: 11717359</identifier><language>eng</language><publisher>United States: Soc Neuroscience</publisher><subject>Adaptor Proteins, Signal Transducing ; Animals ; Behavior, Animal - physiology ; Biomarkers ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Carrier Proteins - metabolism ; Electrophysiology ; Guanosine Triphosphate - metabolism ; Helminth Proteins - genetics ; Helminth Proteins - metabolism ; Locomotion - genetics ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Phenotype ; Physical Stimulation ; Protein Structure, Tertiary - physiology ; rab GTP-Binding Proteins - genetics ; rab GTP-Binding Proteins - metabolism ; rab3 GTP-Binding Proteins - genetics ; rab3 GTP-Binding Proteins - metabolism ; Rabphilin-3A ; Sequence Deletion ; Sequence Homology, Amino Acid ; Sleep Stages - genetics ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; Synapses - metabolism ; Synaptic Vesicles - metabolism ; Synaptosomal-Associated Protein 25 ; Vesicular Transport Proteins</subject><ispartof>The Journal of neuroscience, 2001-12, Vol.21 (23), p.9255-9264</ispartof><rights>Copyright © 2001 Society for Neuroscience 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-c71f3c6486012b3a81ac4dd7bfda49a0d5a627c158131690493173840359abe23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6763921/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6763921/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11717359$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Staunton, Jane</creatorcontrib><creatorcontrib>Ganetzky, Barry</creatorcontrib><creatorcontrib>Nonet, Michael L</creatorcontrib><title>Rabphilin Potentiates Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Function Independently of rab3</title><title>The Journal of neuroscience</title><addtitle>J Neurosci</addtitle><description>Rabphilin, a putative rab effector, interacts specifically with the GTP-bound form of the synaptic vesicle-associated protein rab3a. In this study, we define in vivo functions for rabphilin through the characterization of mutants that disrupt the Caenorhabditis elegans rabphilin homolog. The mutants do not display the general synaptic defects associated with rab3 lesions, as assayed at the pharmacological, physiological, and ultrastructural level. However, rabphilin mutants exhibit severe lethargy in the absence of mechanical stimulation. Furthermore, rabphilin mutations display strong synergistic interactions with hypomorphic lesions in the syntaxin, synaptosomal-associated protein of 25 kDa, and synaptobrevin soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) genes; double mutants were nonresponsive to mechanical stimulation. These synergistic interactions were independent of rab3 function and were not observed in rab3-SNARE double mutants. Our data reveal rab3-independent functions for rabphilin in the potentiation of SNARE function.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Behavior, Animal - physiology</subject><subject>Biomarkers</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Carrier Proteins - metabolism</subject><subject>Electrophysiology</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - metabolism</subject><subject>Locomotion - genetics</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Phenotype</subject><subject>Physical Stimulation</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>rab GTP-Binding Proteins - genetics</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>rab3 GTP-Binding Proteins - genetics</subject><subject>rab3 GTP-Binding Proteins - metabolism</subject><subject>Rabphilin-3A</subject><subject>Sequence Deletion</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sleep Stages - genetics</subject><subject>SNARE Proteins</subject><subject>Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins</subject><subject>Synapses - metabolism</subject><subject>Synaptic Vesicles - metabolism</subject><subject>Synaptosomal-Associated Protein 25</subject><subject>Vesicular Transport Proteins</subject><issn>0270-6474</issn><issn>1529-2401</issn><issn>1529-2401</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVFv0zAUhS0EYmXwF1DEAzyl-NpJnPCANFXtVjRtU8ueLcdxFiMn7mxnVfn1OLQa8MSLr6x77qdzdBD6AHgOOaGfv90s7ze328V6TiAlNMUVyfM5wRheoFlUVCnJMLxEM0wYTouMZWfojfc_MMYMA3uNzgAYMJpXM_RzI-pdp40ekjsb1BC0CMonW2vG2qjkJl2G7mB6YZTudaOSrRq8DvpJJSshg3XJRQhCdn28TO5cJETQRkm1m3arcZBB2yFZD43aqfgMwRwS2yZO1PQtetUK49W70zxH96vl98VVen17uV5cXKcyozSkkkFLZZGVBQZSU1GCkFnTsLptRFYJ3OSiIExCXgKFosJZRWO2MsMxn6gVoefo65G7G-teNTKacMLwndO9cAduheb_bgbd8Qf7xAtW0IpABHw8AZx9HJUPvNdeKmPEoOzoOSOkymnJ_isElpcVLiZLX45C6az3TrXPbgDzqWP-3DEnwOP_d8d86jgev_87z5_TU6lR8Oko6PRDt9dOcR8LNFEOfL_fH4ETj_4C9Amz-w</recordid><startdate>20011201</startdate><enddate>20011201</enddate><creator>Staunton, Jane</creator><creator>Ganetzky, Barry</creator><creator>Nonet, Michael L</creator><general>Soc Neuroscience</general><general>Society for Neuroscience</general><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>7TK</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20011201</creationdate><title>Rabphilin Potentiates Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Function Independently of rab3</title><author>Staunton, Jane ; Ganetzky, Barry ; Nonet, Michael L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-c71f3c6486012b3a81ac4dd7bfda49a0d5a627c158131690493173840359abe23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Behavior, Animal - physiology</topic><topic>Biomarkers</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>Electrophysiology</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - metabolism</topic><topic>Locomotion - genetics</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Phenotype</topic><topic>Physical Stimulation</topic><topic>Protein Structure, Tertiary - physiology</topic><topic>rab GTP-Binding Proteins - genetics</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>rab3 GTP-Binding Proteins - genetics</topic><topic>rab3 GTP-Binding Proteins - metabolism</topic><topic>Rabphilin-3A</topic><topic>Sequence Deletion</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sleep Stages - genetics</topic><topic>SNARE Proteins</topic><topic>Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins</topic><topic>Synapses - metabolism</topic><topic>Synaptic Vesicles - metabolism</topic><topic>Synaptosomal-Associated Protein 25</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Staunton, Jane</creatorcontrib><creatorcontrib>Ganetzky, Barry</creatorcontrib><creatorcontrib>Nonet, Michael L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Staunton, Jane</au><au>Ganetzky, Barry</au><au>Nonet, Michael L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rabphilin Potentiates Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Function Independently of rab3</atitle><jtitle>The Journal of neuroscience</jtitle><addtitle>J Neurosci</addtitle><date>2001-12-01</date><risdate>2001</risdate><volume>21</volume><issue>23</issue><spage>9255</spage><epage>9264</epage><pages>9255-9264</pages><issn>0270-6474</issn><issn>1529-2401</issn><eissn>1529-2401</eissn><abstract>Rabphilin, a putative rab effector, interacts specifically with the GTP-bound form of the synaptic vesicle-associated protein rab3a. In this study, we define in vivo functions for rabphilin through the characterization of mutants that disrupt the Caenorhabditis elegans rabphilin homolog. The mutants do not display the general synaptic defects associated with rab3 lesions, as assayed at the pharmacological, physiological, and ultrastructural level. However, rabphilin mutants exhibit severe lethargy in the absence of mechanical stimulation. Furthermore, rabphilin mutations display strong synergistic interactions with hypomorphic lesions in the syntaxin, synaptosomal-associated protein of 25 kDa, and synaptobrevin soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) genes; double mutants were nonresponsive to mechanical stimulation. These synergistic interactions were independent of rab3 function and were not observed in rab3-SNARE double mutants. 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| subjects | Adaptor Proteins, Signal Transducing Animals Behavior, Animal - physiology Biomarkers Caenorhabditis elegans Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Carrier Proteins - metabolism Electrophysiology Guanosine Triphosphate - metabolism Helminth Proteins - genetics Helminth Proteins - metabolism Locomotion - genetics Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Mutagenesis, Site-Directed Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Phenotype Physical Stimulation Protein Structure, Tertiary - physiology rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism rab3 GTP-Binding Proteins - genetics rab3 GTP-Binding Proteins - metabolism Rabphilin-3A Sequence Deletion Sequence Homology, Amino Acid Sleep Stages - genetics SNARE Proteins Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Synapses - metabolism Synaptic Vesicles - metabolism Synaptosomal-Associated Protein 25 Vesicular Transport Proteins |
| title | Rabphilin Potentiates Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Function Independently of rab3 |
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