Neurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin
A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins we...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1992-07, Vol.257 (5066), p.50-56 |
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| creator | Ushkaryov, Yuri A. Petrenko, Alexander G. Geppert, Martin Südhof, Thomas C. |
| description | A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for α-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal. |
| doi_str_mv | 10.1126/science.1621094 |
| format | Article |
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At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for α-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1621094</identifier><identifier>PMID: 1621094</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>alpha -latrotoxin ; Alternative splicing ; Amino Acid Isomerases - genetics ; Amino Acid Sequence ; Amino acids ; Animals ; Antibodies ; Araneae ; Biological and medical sciences ; Carrier Proteins - genetics ; cDNA ; Cell coat. Cell surface ; Cell structures and functions ; Cellular recognition ; Cloning, Molecular ; Complementary DNA ; COS cells ; Cyclosporins - metabolism ; DNA - genetics ; Exons ; Fundamental and applied biological sciences. Psychology ; genes ; homology ; laminin ; Laminin - genetics ; Latrodectus mactans ; localization ; Membrane proteins ; Molecular and cellular biology ; Molecular Sequence Data ; Nerve proteins ; Nerve tissue proteins ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; neurexin ; Neurons ; nucleotide sequence ; Organ Specificity ; PC12 Cells ; Peptidylprolyl Isomerase ; Polymerase Chain Reaction ; predictions ; Rats ; Receptors ; Receptors, Cholinergic - genetics ; Receptors, Peptide ; RNA ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sequence Homology, Nucleic Acid ; Spider Venoms - metabolism ; splicing ; Synapses - physiology ; Theridiidae</subject><ispartof>Science (American Association for the Advancement of Science), 1992-07, Vol.257 (5066), p.50-56</ispartof><rights>Copyright 1992 American Association for the Advancement of Science</rights><rights>1992 INIST-CNRS</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1992 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c646t-9f6ab3690862cce28407ea83a881c0cc8b7ee25146db421efd1b697dd12b415d3</citedby><cites>FETCH-LOGICAL-c646t-9f6ab3690862cce28407ea83a881c0cc8b7ee25146db421efd1b697dd12b415d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2877428$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2877428$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5405151$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1621094$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ushkaryov, Yuri A.</creatorcontrib><creatorcontrib>Petrenko, Alexander G.</creatorcontrib><creatorcontrib>Geppert, Martin</creatorcontrib><creatorcontrib>Südhof, Thomas C.</creatorcontrib><title>Neurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for α-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.</description><subject>alpha -latrotoxin</subject><subject>Alternative splicing</subject><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Araneae</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>cDNA</subject><subject>Cell coat. Cell surface</subject><subject>Cell structures and functions</subject><subject>Cellular recognition</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>COS cells</subject><subject>Cyclosporins - metabolism</subject><subject>DNA - genetics</subject><subject>Exons</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>homology</subject><subject>laminin</subject><subject>Laminin - genetics</subject><subject>Latrodectus mactans</subject><subject>localization</subject><subject>Membrane proteins</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Nerve proteins</subject><subject>Nerve tissue proteins</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>neurexin</subject><subject>Neurons</subject><subject>nucleotide sequence</subject><subject>Organ Specificity</subject><subject>PC12 Cells</subject><subject>Peptidylprolyl Isomerase</subject><subject>Polymerase Chain Reaction</subject><subject>predictions</subject><subject>Rats</subject><subject>Receptors</subject><subject>Receptors, Cholinergic - genetics</subject><subject>Receptors, Peptide</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Spider Venoms - metabolism</subject><subject>splicing</subject><subject>Synapses - physiology</subject><subject>Theridiidae</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0s-L1DAUB_Aiyjqunr0o5CDiYbubH22aelsHnV0oO-KoFw8lTV_HLG0yJins_ln-I_5NRqbMMjDgkMODfD8JJO8lyUuCzwmh_MIrDUbBOeGU4DJ7lMxiydOSYvY4mWHMeCpwkT9Nnnl_i3HMSnaSnEx8lvy4gdHBnTb-PVrdG7kJWqE59D1aja6TCtBnZwPEHH2BXgZoUbAo_AT053dayRBDG0_HUMEmWIekaVElB220eZ486WTv4cVUT5Nvnz5-nV-l1XJxPb-sUsUzHtKy47JhvMSCU6WAigwXIAWTQhCFlRJNAUBzkvG2ySiBriUNL4u2JbTJSN6y0-Tt9t6Ns79G8KEetFfxDdKAHX1dMJwTKvL_wvgrBeM5jvBsC9eyh1qbzgYn1RoMONlbA52O25eEsrLMKI88PcDjamHQ6pB_t-cjCXAX1nL0vr5e3RxNl9-Pph8Wx1KxqPbo2SGqbN_DGurYyPlyj19suXLWewddvXF6kO6-Jrj-N7H1NLH1NILxxOupKWMzQPvgd_mbKZdeyb5z0ijtdyzPYnNzEtmrLbv1cQx3MRVFkVHB_gKAAvnC</recordid><startdate>19920703</startdate><enddate>19920703</enddate><creator>Ushkaryov, Yuri A.</creator><creator>Petrenko, Alexander G.</creator><creator>Geppert, Martin</creator><creator>Südhof, Thomas C.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>7QL</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19920703</creationdate><title>Neurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin</title><author>Ushkaryov, Yuri A. ; Petrenko, Alexander G. ; Geppert, Martin ; Südhof, Thomas C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c646t-9f6ab3690862cce28407ea83a881c0cc8b7ee25146db421efd1b697dd12b415d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>alpha -latrotoxin</topic><topic>Alternative splicing</topic><topic>Amino Acid Isomerases - genetics</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Araneae</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>cDNA</topic><topic>Cell coat. Cell surface</topic><topic>Cell structures and functions</topic><topic>Cellular recognition</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>COS cells</topic><topic>Cyclosporins - metabolism</topic><topic>DNA - genetics</topic><topic>Exons</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>homology</topic><topic>laminin</topic><topic>Laminin - genetics</topic><topic>Latrodectus mactans</topic><topic>localization</topic><topic>Membrane proteins</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Nerve proteins</topic><topic>Nerve tissue proteins</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>neurexin</topic><topic>Neurons</topic><topic>nucleotide sequence</topic><topic>Organ Specificity</topic><topic>PC12 Cells</topic><topic>Peptidylprolyl Isomerase</topic><topic>Polymerase Chain Reaction</topic><topic>predictions</topic><topic>Rats</topic><topic>Receptors</topic><topic>Receptors, Cholinergic - genetics</topic><topic>Receptors, Peptide</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Spider Venoms - metabolism</topic><topic>splicing</topic><topic>Synapses - physiology</topic><topic>Theridiidae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ushkaryov, Yuri A.</creatorcontrib><creatorcontrib>Petrenko, Alexander G.</creatorcontrib><creatorcontrib>Geppert, Martin</creatorcontrib><creatorcontrib>Südhof, Thomas C.</creatorcontrib><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>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ushkaryov, Yuri A.</au><au>Petrenko, Alexander G.</au><au>Geppert, Martin</au><au>Südhof, Thomas C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1992-07-03</date><risdate>1992</risdate><volume>257</volume><issue>5066</issue><spage>50</spage><epage>56</epage><pages>50-56</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for α-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1621094</pmid><doi>10.1126/science.1621094</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1992-07, Vol.257 (5066), p.50-56 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73051285 |
| source | Jstor Complete Legacy; MEDLINE; Science Magazine |
| subjects | alpha -latrotoxin Alternative splicing Amino Acid Isomerases - genetics Amino Acid Sequence Amino acids Animals Antibodies Araneae Biological and medical sciences Carrier Proteins - genetics cDNA Cell coat. Cell surface Cell structures and functions Cellular recognition Cloning, Molecular Complementary DNA COS cells Cyclosporins - metabolism DNA - genetics Exons Fundamental and applied biological sciences. Psychology genes homology laminin Laminin - genetics Latrodectus mactans localization Membrane proteins Molecular and cellular biology Molecular Sequence Data Nerve proteins Nerve tissue proteins Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics neurexin Neurons nucleotide sequence Organ Specificity PC12 Cells Peptidylprolyl Isomerase Polymerase Chain Reaction predictions Rats Receptors Receptors, Cholinergic - genetics Receptors, Peptide RNA RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Homology, Nucleic Acid Spider Venoms - metabolism splicing Synapses - physiology Theridiidae |
| title | Neurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin |
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