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  PtdInsP(2) and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium.

Perez-Lara, A., Thapa, A., Nyenhuis, S. B., Nyenhuis, D. A., Halder, P., Tietzel, M., et al. (2016). PtdInsP(2) and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium. eLife, 5: e15886. doi:10.7554/eLife.15886.001.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2DDB-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2DDF-A
Genre: Journal Article

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Perez-Lara, A.1, Author              
Thapa, A., Author
Nyenhuis, S. B., Author
Nyenhuis, D. A., Author
Halder, P.1, Author              
Tietzel, M., Author
Tittmann, K., Author
Cafiso, D. S., Author
Jahn, R.1, Author              
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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 Abstract: The Ca2+-sensor synaptotagmin-1 that triggers neuronal exocytosis binds to negatively charged membrane lipids (mainly phosphatidylserine (PtdSer) and phosphoinositides (Ptdlns)) but the molecular details of this process are not fully understood. Using quantitative thermodynamic, kinetic and structural methods, we show that synaptotagmin-1 (from Rattus norvegicus and expressed in Escherichia coli) binds to Ptdlns(4,5)P-2 via a polybasic lysine patch in the C2B domain, which may promote the priming or docking of synaptic vesicles. Ca2+ neutralizes the negative charges of the Ca2+-binding sites, resulting in the penetration of synaptotagmin-1 into the membrane, via binding of PtdSer, and an increase in the affinity of the polybasic lysine patch to phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P-2). These Ca2+-induced events decrease the dissociation rate of synaptotagmin-1 membrane binding while the association rate remains unchanged. We conclude that both membrane penetration and the increased residence time of synaptotagmin-1 at the plasma membrane are crucial for triggering exocytotic membrane fusion.

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Language(s): eng - English
 Dates: 2016-10-28
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.15886.001
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Title: eLife
Source Genre: Journal
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Pages: 22 Volume / Issue: 5 Sequence Number: e15886 Start / End Page: - Identifier: -