Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process
Syntaxin-1 is a component of the synaptic vesicle docking and/or fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 1998-05, Vol.20 (5), p.905-915 |
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| creator | Fujita, Yasuyuki Shirataki, Hiromichi Sakisaka, Toshiaki Asakura, Takeshi Ohya, Takeshi Kotani, Hirokazu Yokoyama, Shigekazu Nishioka, Hideo Matsuura, Yoshiharu Mizoguchi, Akira Scheller, Richard H Takai, Yoshimi |
| description | Syntaxin-1 is a component of the synaptic vesicle docking and/or fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and 20S complexes. In this report, we identify a novel syntaxin-1–binding protein, tomosyn, that is capable of dissociating Munc18 from syntaxin-1 and forming a novel 10S complex with syntaxin-1, synaptosome-associated protein of 25 kDa (SNAP-25), and synaptotagmin. The 130 kDa isoform of tomosyn is specifically expressed in brain, where its distribution partly overlaps with that of syntaxin-1 in nerve terminals. High level expression of either syntaxin-1 or tomosyn results in a specific reduction in Ca
2+-dependent exocytosis from PC12 cells. These results suggest that tomosyn is an important component in the neurotransmitter release process where it may stimulate SNARE complex formation. |
| doi_str_mv | 10.1016/S0896-6273(00)80472-9 |
| format | Article |
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2+-dependent exocytosis from PC12 cells. These results suggest that tomosyn is an important component in the neurotransmitter release process where it may stimulate SNARE complex formation.</description><identifier>ISSN: 0896-6273</identifier><identifier>EISSN: 1097-4199</identifier><identifier>DOI: 10.1016/S0896-6273(00)80472-9</identifier><identifier>PMID: 9620695</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antigens, Surface - chemistry ; Antigens, Surface - metabolism ; Blotting, Western ; Brain Chemistry ; Calcium - physiology ; Carrier Proteins - analysis ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cloning, Molecular ; COS Cells - physiology ; DNA, Complementary ; Exocytosis - physiology ; Isomerism ; Molecular Sequence Data ; Munc18 Proteins ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neurons - chemistry ; Neurons - cytology ; Neurons - metabolism ; Neuropeptides - analysis ; Neuropeptides - genetics ; Neuropeptides - metabolism ; Neurotransmitter Agents - metabolism ; PC12 Cells ; Protein Binding - physiology ; R-SNARE Proteins ; Rats ; SNARE complex ; Synaptic Transmission - physiology ; Syntaxin 1 ; tomosyn ; Vesicular Transport Proteins</subject><ispartof>Neuron (Cambridge, Mass.), 1998-05, Vol.20 (5), p.905-915</ispartof><rights>1998 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-fbbf54785abb9bef7f76dcce02e2da3a5bc093387a27758f3eca787b73c333f23</citedby><cites>FETCH-LOGICAL-c461t-fbbf54785abb9bef7f76dcce02e2da3a5bc093387a27758f3eca787b73c333f23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0896627300804729$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9620695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fujita, Yasuyuki</creatorcontrib><creatorcontrib>Shirataki, Hiromichi</creatorcontrib><creatorcontrib>Sakisaka, Toshiaki</creatorcontrib><creatorcontrib>Asakura, Takeshi</creatorcontrib><creatorcontrib>Ohya, Takeshi</creatorcontrib><creatorcontrib>Kotani, Hirokazu</creatorcontrib><creatorcontrib>Yokoyama, Shigekazu</creatorcontrib><creatorcontrib>Nishioka, Hideo</creatorcontrib><creatorcontrib>Matsuura, Yoshiharu</creatorcontrib><creatorcontrib>Mizoguchi, Akira</creatorcontrib><creatorcontrib>Scheller, Richard H</creatorcontrib><creatorcontrib>Takai, Yoshimi</creatorcontrib><title>Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process</title><title>Neuron (Cambridge, Mass.)</title><addtitle>Neuron</addtitle><description>Syntaxin-1 is a component of the synaptic vesicle docking and/or fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and 20S complexes. In this report, we identify a novel syntaxin-1–binding protein, tomosyn, that is capable of dissociating Munc18 from syntaxin-1 and forming a novel 10S complex with syntaxin-1, synaptosome-associated protein of 25 kDa (SNAP-25), and synaptotagmin. The 130 kDa isoform of tomosyn is specifically expressed in brain, where its distribution partly overlaps with that of syntaxin-1 in nerve terminals. High level expression of either syntaxin-1 or tomosyn results in a specific reduction in Ca
2+-dependent exocytosis from PC12 cells. These results suggest that tomosyn is an important component in the neurotransmitter release process where it may stimulate SNARE complex formation.</description><subject>Animals</subject><subject>Antigens, Surface - chemistry</subject><subject>Antigens, Surface - metabolism</subject><subject>Blotting, Western</subject><subject>Brain Chemistry</subject><subject>Calcium - physiology</subject><subject>Carrier Proteins - analysis</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cloning, Molecular</subject><subject>COS Cells - physiology</subject><subject>DNA, Complementary</subject><subject>Exocytosis - physiology</subject><subject>Isomerism</subject><subject>Molecular Sequence Data</subject><subject>Munc18 Proteins</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - chemistry</subject><subject>Neurons - cytology</subject><subject>Neurons - metabolism</subject><subject>Neuropeptides - analysis</subject><subject>Neuropeptides - genetics</subject><subject>Neuropeptides - metabolism</subject><subject>Neurotransmitter Agents - metabolism</subject><subject>PC12 Cells</subject><subject>Protein Binding - physiology</subject><subject>R-SNARE Proteins</subject><subject>Rats</subject><subject>SNARE complex</subject><subject>Synaptic Transmission - physiology</subject><subject>Syntaxin 1</subject><subject>tomosyn</subject><subject>Vesicular Transport Proteins</subject><issn>0896-6273</issn><issn>1097-4199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkElOxDAQRS0EgmY4ApJXCBYBO07imA2CFpPUahDD2nKcChgldmO7Eb3jDtyQk5AexJZVLf77VaqH0D4lx5TQ4uSRlKJIipSzQ0KOSpLxNBFraECJ4ElGhVhHgz9kC22H8EYIzXJBN9GmKFJSiHyA3p5c58LMnmKFH2c2qk9jE_rz9X1hbG3sC773LoKxOL6qiK-c70JPjt0HtHjoukkLn3iRAh7DtGe9sqEzMYLHD9CCCjBfoSGEXbTRqDbA3mruoOery6fhTTK6u74dno8SnRU0Jk1VNXnGy1xVlaig4Q0vaq2BpJDWiqm80kQwVnKVcp6XDQOteMkrzjRjrEnZDjpY7p149z6FEGVngoa2VRbcNEjKCesd0R7Ml6D2LgQPjZx40yk_k5TIuWO5cCznAiUhcuFYir63vzowrTqo_1orqX1-tsyh__LDgJdBG7AaauNBR1k788-FX9cFjkc</recordid><startdate>19980501</startdate><enddate>19980501</enddate><creator>Fujita, Yasuyuki</creator><creator>Shirataki, Hiromichi</creator><creator>Sakisaka, Toshiaki</creator><creator>Asakura, Takeshi</creator><creator>Ohya, Takeshi</creator><creator>Kotani, Hirokazu</creator><creator>Yokoyama, Shigekazu</creator><creator>Nishioka, Hideo</creator><creator>Matsuura, Yoshiharu</creator><creator>Mizoguchi, Akira</creator><creator>Scheller, Richard H</creator><creator>Takai, Yoshimi</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>7TK</scope></search><sort><creationdate>19980501</creationdate><title>Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process</title><author>Fujita, Yasuyuki ; Shirataki, Hiromichi ; Sakisaka, Toshiaki ; Asakura, Takeshi ; Ohya, Takeshi ; Kotani, Hirokazu ; Yokoyama, Shigekazu ; Nishioka, Hideo ; Matsuura, Yoshiharu ; Mizoguchi, Akira ; Scheller, Richard H ; Takai, Yoshimi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-fbbf54785abb9bef7f76dcce02e2da3a5bc093387a27758f3eca787b73c333f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Antigens, Surface - chemistry</topic><topic>Antigens, Surface - metabolism</topic><topic>Blotting, Western</topic><topic>Brain Chemistry</topic><topic>Calcium - physiology</topic><topic>Carrier Proteins - analysis</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cloning, Molecular</topic><topic>COS Cells - physiology</topic><topic>DNA, Complementary</topic><topic>Exocytosis - physiology</topic><topic>Isomerism</topic><topic>Molecular Sequence Data</topic><topic>Munc18 Proteins</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons - chemistry</topic><topic>Neurons - cytology</topic><topic>Neurons - metabolism</topic><topic>Neuropeptides - analysis</topic><topic>Neuropeptides - genetics</topic><topic>Neuropeptides - metabolism</topic><topic>Neurotransmitter Agents - metabolism</topic><topic>PC12 Cells</topic><topic>Protein Binding - physiology</topic><topic>R-SNARE Proteins</topic><topic>Rats</topic><topic>SNARE complex</topic><topic>Synaptic Transmission - physiology</topic><topic>Syntaxin 1</topic><topic>tomosyn</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fujita, Yasuyuki</creatorcontrib><creatorcontrib>Shirataki, Hiromichi</creatorcontrib><creatorcontrib>Sakisaka, Toshiaki</creatorcontrib><creatorcontrib>Asakura, Takeshi</creatorcontrib><creatorcontrib>Ohya, Takeshi</creatorcontrib><creatorcontrib>Kotani, Hirokazu</creatorcontrib><creatorcontrib>Yokoyama, Shigekazu</creatorcontrib><creatorcontrib>Nishioka, Hideo</creatorcontrib><creatorcontrib>Matsuura, Yoshiharu</creatorcontrib><creatorcontrib>Mizoguchi, Akira</creatorcontrib><creatorcontrib>Scheller, Richard H</creatorcontrib><creatorcontrib>Takai, Yoshimi</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>Neurosciences Abstracts</collection><jtitle>Neuron (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fujita, Yasuyuki</au><au>Shirataki, Hiromichi</au><au>Sakisaka, Toshiaki</au><au>Asakura, Takeshi</au><au>Ohya, Takeshi</au><au>Kotani, Hirokazu</au><au>Yokoyama, Shigekazu</au><au>Nishioka, Hideo</au><au>Matsuura, Yoshiharu</au><au>Mizoguchi, Akira</au><au>Scheller, Richard H</au><au>Takai, Yoshimi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process</atitle><jtitle>Neuron (Cambridge, Mass.)</jtitle><addtitle>Neuron</addtitle><date>1998-05-01</date><risdate>1998</risdate><volume>20</volume><issue>5</issue><spage>905</spage><epage>915</epage><pages>905-915</pages><issn>0896-6273</issn><eissn>1097-4199</eissn><abstract>Syntaxin-1 is a component of the synaptic vesicle docking and/or fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and 20S complexes. In this report, we identify a novel syntaxin-1–binding protein, tomosyn, that is capable of dissociating Munc18 from syntaxin-1 and forming a novel 10S complex with syntaxin-1, synaptosome-associated protein of 25 kDa (SNAP-25), and synaptotagmin. The 130 kDa isoform of tomosyn is specifically expressed in brain, where its distribution partly overlaps with that of syntaxin-1 in nerve terminals. High level expression of either syntaxin-1 or tomosyn results in a specific reduction in Ca
2+-dependent exocytosis from PC12 cells. These results suggest that tomosyn is an important component in the neurotransmitter release process where it may stimulate SNARE complex formation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9620695</pmid><doi>10.1016/S0896-6273(00)80472-9</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Neuron (Cambridge, Mass.), 1998-05, Vol.20 (5), p.905-915 |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Antigens, Surface - chemistry Antigens, Surface - metabolism Blotting, Western Brain Chemistry Calcium - physiology Carrier Proteins - analysis Carrier Proteins - genetics Carrier Proteins - metabolism Cloning, Molecular COS Cells - physiology DNA, Complementary Exocytosis - physiology Isomerism Molecular Sequence Data Munc18 Proteins Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neurons - chemistry Neurons - cytology Neurons - metabolism Neuropeptides - analysis Neuropeptides - genetics Neuropeptides - metabolism Neurotransmitter Agents - metabolism PC12 Cells Protein Binding - physiology R-SNARE Proteins Rats SNARE complex Synaptic Transmission - physiology Syntaxin 1 tomosyn Vesicular Transport Proteins |
| title | Tomosyn: a Syntaxin-1–Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process |
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