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  Superpriming of synaptic vesicles after their recruitment to the readily releasable pool.

Lee, J. S., Ho, W. K., Neher, E., & Lee, S. H. (2013). Superpriming of synaptic vesicles after their recruitment to the readily releasable pool. Proceedings of the National Academy of Sciences of the United States of America, 110(37), 15079-15084. doi:10.1073/pnas.1314427110.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-628D-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-80EE-B
Genre: Journal Article

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Lee, J. S., Author
Ho, W. K., Author
Neher, E.1, Author              
Lee, S. H., Author
Affiliations:
1Emeritus Group of Membrane Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_1571137              

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Free keywords: presynaptic; vesicle release rate constant; phospholipase C; diacylglycerol; calyx of Held
 Abstract: Recruitment of release-competent vesicles during sustained synaptic activity is one of the major factors governing short-term plasticity. During bursts of synaptic activity, vesicles are recruited to a fast-releasing pool from a reluctant vesicle pool through an actin-dependent mechanism. We now show that newly recruited vesicles in the fast-releasing pool do not respond at full speed to a strong Ca2+ stimulus, but require approximately 4 s to mature to a "superprimed" state. Superpriming was found to be altered by agents that modulate the function of unc13 homolog proteins (Munc13s), but not by calmodulin inhibitors or actin-disrupting agents. These findings indicate that recruitment and superpriming of vesicles are regulated by separate mechanisms, which require integrity of the cytoskeleton and activation of Munc13s, respectively. We propose that refilling of the fast-releasing vesicle pool proceeds in two steps, rapid actin-dependent "positional priming," which brings vesicles closer to Ca2+ sources, followed by slower superpriming, which enhances the Ca2+ sensitivity of primed vesicles.

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Language(s): eng - English
 Dates: 2013-08-262013-09-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1314427110
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 110 (37) Sequence Number: - Start / End Page: 15079 - 15084 Identifier: ISSN: 0027-8424