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  Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.

Honigmann, A., van den Bogaart, G., Iraheta, E., Risselada, H. J., Milovanovic, D., Müller, V., et al. (2013). Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment. Nature Structural and Molecular Biology, 20, 679-686. doi:10.1038/nsmb.2570.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-7673-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CEEB-4
Genre: Journal Article

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 Creators:
Honigmann, A.1, Author              
van den Bogaart, G.2, Author              
Iraheta, E., Author
Risselada, H. J.3, Author              
Milovanovic, D.1, Author              
Müller, V.1, Author              
Müller, S., Author
Diederichsen, U., Author
Fasshauer, D.4, Author              
Grubmüller, H.3, Author              
Hell, S. W.1, Author              
Eggeling, C.1, Author              
Kühnel, K.2, Author              
Jahn, R.2, Author              
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              
2Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
3Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              
4Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578596              

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 Abstract: Synaptic-vesicle exocytosis is mediated by the vesicular Ca2+ sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca2+ through PIP2. This interaction allows both Ca2+-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca2+ triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca2+ influx bringing the vesicle membrane close enough for membrane fusion.

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Language(s): eng - English
 Dates: 2013-05-122013
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2570
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 20 Sequence Number: - Start / End Page: 679 - 686 Identifier: -