Journal
NEURON
Volume 32, Issue 6, Pages 1057-1069Publisher
CELL PRESS
DOI: 10.1016/S0896-6273(01)00548-7
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Funding
- NINDS NIH HHS [NS40944] Funding Source: Medline
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Synaptotagmin 1 probably functions as a Ca2+ sensor in neurotransmitter release via its two C-2-domains, but no common Ca2+-dependent activity that could underlie a cooperative action between them has been described. The NMR structure of the C2B-domain now reveals a beta sandwich that exhibits striking similarities and differences with the C(2)A-domain. Whereas the bottom face of the C2B-domain has two additional a helices that may be involved in specialized Ca2+-independent functions, the top face binds two Ca2+ ions and is remarkably similar to the C(2)A-domain. Consistent with these results, but in contrast to previous studies, we find that the C2B-domain binds phospholipids in a Ca2+-dependent manner similarly to the C(2)A-domain. These results suggest a novel view of synaptotagmin function whereby the two C-2-domains cooperate in a common activity, Ca2+-dependent phospholipid binding, to trigger neurotransmitter release.
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