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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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 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: Issued
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 Rev. Type: 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: -