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JCS ePress online publication date 20 Jun 2006
doi: 10.1242/jcs.03037

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Research Article

Tomosyn-1 is involved in a post-docking event required for pancreatic {beta}-cell exocytosis


Séverine Cheviet, Paola Bezzi, Rosita Ivarsson, Erik Renström, David Viertl, Sandor Kasas, Stefan Catsicas, and Romano Regazzi*
* Author for correspondence (e-mail: Romano.Regazzi{at}unil.ch)

Although the assembly of a ternary complex between the SNARE proteins syntaxin-1, SNAP25 and VAMP2 is known to be crucial for insulin exocytosis, the mechanisms controlling this key event are poorly understood. We found that pancreatic {beta}-cells express different isoforms of tomosyn-1, a syntaxin-1-binding protein possessing a SNARE-like motif. Using atomic force microscopy we show that the SNARE-like domain of tomosyn-1 can form a complex with syntaxin-1 and SNAP25 but displays binding forces that are weaker than those observed for VAMP2 (237±13 versus 279±3 pN). In pancreatic {beta}-cells tomosyn-1 was found to be concentrated in cellular compartments enriched in insulin-containing secretory granules. Silencing of tomosyn-1 in the rat {beta}-cell line INS-1E by RNA interference did not affect the number of secretory granules docked at the plasma membrane but led to a reduction in stimulus-induced exocytosis. Replacement of endogenous tomosyn-1 with mouse tomosyn-1, which differs in the nucleotide sequence from its rat homologue and escapes silencing, restored a normal secretory rate. Taken together, our data suggest that tomosyn-1 is involved in a post-docking event that prepares secretory granules for fusion and is necessary to sustain exocytosis of pancreatic {beta}-cells in response to insulin secretagogues.
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