Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation

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Somanath, S., Partridge, C.J., Marshall, C., Rowe, T. and Turner, M.D. ORCID: 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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Official URL: http://doi.org/10.1016/j.bbrc.2016.02.123

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