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Somanath, S, Partridge, CJ, Marshall, C, Rowe, T and Turner, MD 
ORCID: https://orcid.org/0000-0001-7175-1053,
2016.
Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.
Biochemical and Biophysical Research Communications, 473 (2), pp. 403-407.
ISSN 0006-291X
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Abstract
Secretory granule exocytosis is a tightly regulated process requiring granule targeting, tethering, priming, and membrane fusion. At the heart of this process is the SNARE complex, which drives fusion through a coiled-coil zippering effect mediated by the granule v-SNARE protein, VAMP2, and the plasma membrane t-SNAREs, SNAP-25 and syntaxin-1A. Here we demonstrate that in pancreatic β-cells the SNAP-25 accessory protein, snapin, C-terminal H2 domain binds SNAP-25 through its Nterminal Sn-1 domain. Interestingly whilst snapin binds SNAP-25, there is only modest binding of this complex with syntaxin-1A under resting conditions. Instead synataxin-1A appears to be recruited in response to secretory stimulation. These results indicate that snapin plays a role in tethering insulin granules to the plasma membrane through coiled coil interaction of snapin with SNAP-25, with full granule fusion competency only resulting after subsequent syntaxin-1A recruitment triggered by secretory stimulation.
| Item Type: | Journal article |
|---|---|
| Publication Title: | Biochemical and Biophysical Research Communications |
| Creators: | Somanath, S., Partridge, C.J., Marshall, C., Rowe, T. and Turner, M.D. |
| Publisher: | Elsevier |
| Date: | 29 April 2016 |
| Volume: | 473 |
| Number: | 2 |
| ISSN: | 0006-291X |
| Identifiers: | Number Type 10.1016/j.bbrc.2016.02.123 DOI |
| Divisions: | Schools > School of Science and Technology |
| Record created by: | Linda Sullivan |
| Date Added: | 22 Mar 2016 09:04 |
| Last Modified: | 09 Jun 2017 14:00 |
| URI: | https://irep.ntu.ac.uk/id/eprint/27189 |
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