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Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening. | LitMetric

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.

Sci Rep

1] Department of Biochemistry, Biophysics &Molecular Biology, Iowa State University, Ames, Iowa 50011, USA [2] Biomedical Research Institute, Korea Institute of Science and Technology (KIST), Hwarangno 14-gil 6, Seongbuk-gu, Seoul 136-791, South Korea.

Published: March 2015

AI Article Synopsis

Article Abstract

Synaptotagmin 1 (Syt1), a major Ca(2+) sensor in neuroexocytosis, utilizes SNARE- and membrane-binding to regulate vesicle fusion, a required process for neurotransmitter release at the synapse. However, the mechanism by which Syt1 orchestrates SNARE- and membrane- binding to control individual vesicle fusion steps is still unclear. In this study, we used a number of single vesicle assays that can differentiate intermediates of neuroexocytosis, to focus on Syt1 mutants that might impair Syt1-SNARE/PIP2 interaction, Ca(2+)-binding, or membrane penetration. Our results show that, although putative Syt1-SNARE/PIP2 coupling through the polybasic region of the C2B domain is critical for vesicle docking, its disruption does not affect content release. In contrast, Ca(2+)-binding and membrane-penetration mutants significantly reduce content release. Our results thus delineate multiple functions of Syt1 along the pathway of Ca(2+)-triggered exocytosis in unprecedented detail.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4366854PMC
http://dx.doi.org/10.1038/srep09267DOI Listing

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