Differential interaction between the C2B domain of synaptotagmin-I and the Drosophila stonedA and stonedB proteins

Soekmadji, Carolina & Kelly, Leonard E. (2007) Differential interaction between the C2B domain of synaptotagmin-I and the Drosophila stonedA and stonedB proteins. In International Brain Research Organisation Satellite Meeting: Secretory Vesicle Cycle, 9-11 July 2007, Brisbane, Qld.

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Abstract

The stoned locus in Drosophila encodes two proteins StonedA (STNA) and StonedB (STNB), both of which have been suggested to act as adaptins in mediating synaptic vesicle recycling. A combination of immunological, genetic and biochemical studies have shown an interaction of STNA and STNB with the C2B domain of Synaptotagmin-I (SYT-1), an integral synaptic vesicle protein that mediates Ca2+-dependent exocytosis, as well as endocytosis. The C2B domain of SYT-1 contains an AP-2 binding site that controls the size of recycled vesicles, and a C-terminal tryptophan-containing motif that acts as an internalization signal. Investigation of SYT-1 mutations in Drosophila has shown that altering the Ca2+ binding region of the C2B domain, results in a reduction in the rate of vesicle recycling, implicating this region in SYT-I endocytosis.

In this poster, we report the molecular dissection of the interactions between the STNA and STNB proteins and the C2B domain of SYT-1. Deletion of the AP-2 binding site decreased the binding of both STNA and STNB. However, C-terminal deletions of the C2B domain significantly increased STNB binding. In contrast, the same C-terminal deletions reduced the affinity of the C2B domain for STNA. The possible interactions of both STNB and STNA with the Ca2+ binding region of SYT-1 will be also investigated.

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ID Code: 85245
Item Type: Conference Item (Poster)
Refereed: Yes
ISSN: 1530-6860
Divisions: Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Deposited On: 09 Jul 2015 23:17
Last Modified: 09 Jul 2015 23:17

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