A possible docking and fusion particle for synaptic transmission Journal Article
| Authors: | Schiavo, G.; Gmachl, M. J. S.; Stenbeck, G.; Söllner, T. H.; Rothman, J. E. |
| Article Title: | A possible docking and fusion particle for synaptic transmission |
| Abstract: | SEVERAL proteins have been implicated in the rapid (millisecond) calcium-controlled release of transmitters at nerve endings1,2, including soluble NV-ethylmaleimide-sensitive fusion protein (NSF3–5) and soluble NSF attachment protein (±-SNAP3,6), the synaptic SNAP receptor (SNARE)3,7 and the calcium-binding protein synaptotagmin2, which may function as a calcium sensor in exocytosis8. A second SNAP isoform (2-SNAP), which is 83% identical to ±-SNAP, is highly expressed in brain9, but its role is still unclear. Here we show that these proteins assemble cooperatively to form a docking and fusion complex. 2-SNAP (but not ±-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 (2-SNAP) to a calcium sensor (synaptotagmin). Polyphosphoinositols that block transmitter release, inositol 1,3,4,5-tetrakisphosphate (InsP4), inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol 1,2,3,4,5,6-hexakisphosphate (InsP6), also block the assembly of the particle by preventing 2-SNAP from binding to synaptotagmin. © 1995 Nature Publishing Group. |
| Keywords: | nonhuman; animal tissue; nerve tissue proteins; protein binding; membrane proteins; calcium; hybrid protein; recombinant fusion proteins; brain; membrane glycoproteins; carrier proteins; glutathione transferase; calcium-binding proteins; synapse; vesicular transport proteins; calcium ion; synaptic transmission; docking protein; neurotransmitter; snare proteins; priority journal; article; synaptotagmins; inositol polyphosphate; inositol phosphates; n-ethylmaleimide-sensitive proteins; soluble n-ethylmaleimide-sensitive factor attachment proteins; n ethylmaleimide; phytic acid |
| Journal Title: | Nature |
| Volume: | 378 |
| Issue: | 6558 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1995-12-14 |
| Start Page: | 733 |
| End Page: | 736 |
| Language: | English |
| DOI: | 10.1038/378733a0 |
| PUBMED: | 7501022 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 28 August 2018 -- Source: Scopus |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work