Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 97, Issue 11, Pages 5883-5888Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.100127197
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Funding
- NIGMS NIH HHS [R01 GM058183, 1 R01 GM58183-01A1, T32 GM08061, T32 GM008061] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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Synaptotagmin I is a critical component of the synaptic machinery that senses calcium influx and triggers synaptic: vesicle fusion and neurotransmitter release. Fluorescence resonance energy transfer studies conducted on synaptotagmin demonstrate that calcium concentrations required for fusion induce a conformational change (EC50 approximate to 3 mM) that brings the two calcium-binding C2 domains in synaptotagmin closer together. Analytical ultracentrifugation studies reveal that synaptotagmin is monomeric under these conditions, indicating that this calcium-triggered association between the C2 domains is intramolecular, rather than intermolecular. These results suggest a mechanism for synaptotagmin function at the presynaptic plasma membrane that involves the self-association of C2 domains.
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