A possible docking and fusion particle for synaptic transmission
SEVERAL proteins have been implicated in the rapid (millisecond) calcium-controlled release of transmitters at nerve endings 1,2 , including soluble N V-ethylmaleimide-sensitive fusion protein (NSF 3–5 ) and soluble NSF attachment protein (α-SNAP 3,6 ), the synaptic SNAP receptor (SNARE) 3,7 and the...
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| Veröffentlicht in: | Nature (London) 1995-12, Vol.378 (6558), p.733-736 |
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| creator | Schiavo, Giampietro Gmachl, Michael J. S Stenbeck, Gudrun Söllner, Thomas H Rothman, James E |
| description | SEVERAL proteins have been implicated in the rapid (millisecond) calcium-controlled release of transmitters at nerve endings
1,2
, including soluble
N
V-ethylmaleimide-sensitive fusion protein (NSF
3–5
) and soluble NSF attachment protein (α-SNAP
3,6
), the synaptic SNAP receptor (SNARE)
3,7
and the calcium-binding protein synaptotagmin
2
, which may function as a calcium sensor in exocytosis
8
. A second SNAP isoform (β-SNAP), which is 83% identical to α-SNAP, is highly expressed in brain
9
, but its role is still unclear. Here we show that these proteins assemble cooperatively to form a docking and fusion complex. β-SNAP (but not α-SNAP) binds synaptotagmin and recruits NSF, indicating that the complex may link the process of membrane fusion to calcium entry by attaching a specialized fusion protein (β-SNAP) to a calcium sensor (synaptotagmin). Polyphosphoinositols that block transmitter release, inositol 1,3,4,5-tetrakisphosphate (InsP
4
), inositol 1,3,4,5,6-pentakisphosphate (InsP
5
) and inositol 1,2,3,4,5,6-hexakisphosphate (InsP
6
), also block the assembly of the particle by preventing β-SNAP from binding to synaptotagmin. |
| doi_str_mv | 10.1038/378733a0 |
| format | Article |
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1,2
, including soluble
N
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3–5
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3,6
), the synaptic SNAP receptor (SNARE)
3,7
and the calcium-binding protein synaptotagmin
2
, which may function as a calcium sensor in exocytosis
8
. A second SNAP isoform (β-SNAP), which is 83% identical to α-SNAP, is highly expressed in brain
9
, but its role is still unclear. Here we show that these proteins assemble cooperatively to form a docking and fusion complex. β-SNAP (but not α-SNAP) binds synaptotagmin and recruits NSF, indicating that the complex may link the process of membrane fusion to calcium entry by attaching a specialized fusion protein (β-SNAP) to a calcium sensor (synaptotagmin). Polyphosphoinositols that block transmitter release, inositol 1,3,4,5-tetrakisphosphate (InsP
4
), inositol 1,3,4,5,6-pentakisphosphate (InsP
5
) and inositol 1,2,3,4,5,6-hexakisphosphate (InsP
6
), also block the assembly of the particle by preventing β-SNAP from binding to synaptotagmin.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/378733a0</identifier><identifier>PMID: 7501022</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Biochemistry ; Biological and medical sciences ; Calcium ; Calcium - metabolism ; Calcium-Binding Proteins ; Carrier Proteins - metabolism ; Carrier Proteins - physiology ; Fundamental and applied biological sciences. Psychology ; General aspects. Models. Methods ; Glutathione Transferase - metabolism ; Humanities and Social Sciences ; Inositol Phosphates - metabolism ; letter ; Membrane Glycoproteins - metabolism ; Membrane Glycoproteins - physiology ; Membrane Proteins - metabolism ; Membrane Proteins - physiology ; multidisciplinary ; N-Ethylmaleimide-Sensitive Proteins ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - physiology ; Protein Binding ; Proteins ; Recombinant Fusion Proteins - metabolism ; Science ; Science (multidisciplinary) ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; Synaptic Transmission - physiology ; Synaptotagmins ; Vertebrates: nervous system and sense organs ; Vesicular Transport Proteins</subject><ispartof>Nature (London), 1995-12, Vol.378 (6558), p.733-736</ispartof><rights>Springer Nature Limited 1995</rights><rights>1996 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Dec 14, 1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-93cf17eda8b5aed0a6d666b299d1438f1b0e8e0344283050e027d0b01c22bb163</citedby><cites>FETCH-LOGICAL-c550t-93cf17eda8b5aed0a6d666b299d1438f1b0e8e0344283050e027d0b01c22bb163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/378733a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/378733a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,2727,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2926688$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7501022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schiavo, Giampietro</creatorcontrib><creatorcontrib>Gmachl, Michael J. S</creatorcontrib><creatorcontrib>Stenbeck, Gudrun</creatorcontrib><creatorcontrib>Söllner, Thomas H</creatorcontrib><creatorcontrib>Rothman, James E</creatorcontrib><title>A possible docking and fusion particle for synaptic transmission</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>SEVERAL proteins have been implicated in the rapid (millisecond) calcium-controlled release of transmitters at nerve endings
1,2
, including soluble
N
V-ethylmaleimide-sensitive fusion protein (NSF
3–5
) and soluble NSF attachment protein (α-SNAP
3,6
), the synaptic SNAP receptor (SNARE)
3,7
and the calcium-binding protein synaptotagmin
2
, which may function as a calcium sensor in exocytosis
8
. A second SNAP isoform (β-SNAP), which is 83% identical to α-SNAP, is highly expressed in brain
9
, but its role is still unclear. Here we show that these proteins assemble cooperatively to form a docking and fusion complex. β-SNAP (but not α-SNAP) binds synaptotagmin and recruits NSF, indicating that the complex may link the process of membrane fusion to calcium entry by attaching a specialized fusion protein (β-SNAP) to a calcium sensor (synaptotagmin). Polyphosphoinositols that block transmitter release, inositol 1,3,4,5-tetrakisphosphate (InsP
4
), inositol 1,3,4,5,6-pentakisphosphate (InsP
5
) and inositol 1,2,3,4,5,6-hexakisphosphate (InsP
6
), also block the assembly of the particle by preventing β-SNAP from binding to synaptotagmin.</description><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Calcium-Binding Proteins</subject><subject>Carrier Proteins - metabolism</subject><subject>Carrier Proteins - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects. Models. 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S</au><au>Stenbeck, Gudrun</au><au>Söllner, Thomas H</au><au>Rothman, James E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A possible docking and fusion particle for synaptic transmission</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1995-12-14</date><risdate>1995</risdate><volume>378</volume><issue>6558</issue><spage>733</spage><epage>736</epage><pages>733-736</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>SEVERAL proteins have been implicated in the rapid (millisecond) calcium-controlled release of transmitters at nerve endings
1,2
, including soluble
N
V-ethylmaleimide-sensitive fusion protein (NSF
3–5
) and soluble NSF attachment protein (α-SNAP
3,6
), the synaptic SNAP receptor (SNARE)
3,7
and the calcium-binding protein synaptotagmin
2
, which may function as a calcium sensor in exocytosis
8
. A second SNAP isoform (β-SNAP), which is 83% identical to α-SNAP, is highly expressed in brain
9
, but its role is still unclear. Here we show that these proteins assemble cooperatively to form a docking and fusion complex. β-SNAP (but not α-SNAP) binds synaptotagmin and recruits NSF, indicating that the complex may link the process of membrane fusion to calcium entry by attaching a specialized fusion protein (β-SNAP) to a calcium sensor (synaptotagmin). Polyphosphoinositols that block transmitter release, inositol 1,3,4,5-tetrakisphosphate (InsP
4
), inositol 1,3,4,5,6-pentakisphosphate (InsP
5
) and inositol 1,2,3,4,5,6-hexakisphosphate (InsP
6
), also block the assembly of the particle by preventing β-SNAP from binding to synaptotagmin.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7501022</pmid><doi>10.1038/378733a0</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1995-12, Vol.378 (6558), p.733-736 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77753403 |
| source | MEDLINE; Nature; SpringerLink Journals - AutoHoldings |
| subjects | Biochemistry Biological and medical sciences Calcium Calcium - metabolism Calcium-Binding Proteins Carrier Proteins - metabolism Carrier Proteins - physiology Fundamental and applied biological sciences. Psychology General aspects. Models. Methods Glutathione Transferase - metabolism Humanities and Social Sciences Inositol Phosphates - metabolism letter Membrane Glycoproteins - metabolism Membrane Glycoproteins - physiology Membrane Proteins - metabolism Membrane Proteins - physiology multidisciplinary N-Ethylmaleimide-Sensitive Proteins Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Protein Binding Proteins Recombinant Fusion Proteins - metabolism Science Science (multidisciplinary) SNARE Proteins Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Synaptic Transmission - physiology Synaptotagmins Vertebrates: nervous system and sense organs Vesicular Transport Proteins |
| title | A possible docking and fusion particle for synaptic transmission |
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