Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 3, Pages 209-217Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1056
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Funding
- NCRR NIH HHS [P41RR02250] Funding Source: Medline
- NIGMS NIH HHS [GM26494] Funding Source: Medline
- NINDS NIH HHS [NS40944] Funding Source: Medline
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Synaptotagmin acts as a Ca2+ sensor in neurotransmitter release through its two C-2 domains. Ca2+-dependent phospholipid binding is key for synaptotagmin function, but it is unclear how this activity cooperates with the SNARE complex involved in release or why Ca2+ binding to the C2B domain is more crucial for release than Ca2+ binding to the C(2)A domain. Here we show that Ca2+ induces high-affinity simultaneous binding of synaptotagmin to two membranes, bringing them into close proximity. The synaptotagmin C2B domain is sufficient for this ability, which arises from the abundance of basic residues around its surface. We propose a model wherein synaptotagmin cooperates with the SNAREs in bringing the synaptic vesicle and plasma membranes together and accelerates membrane fusion through the highly positive electrostatic potential of its C2B domain.
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