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  Calcium promotes the formation of syntaxin 1 mesoscale domains through phosphatidylinositol 4,5-bisphosphate.

Milovanovic, D., Platen, M., Junius, M., Diederichsen, U., Schaap, I. A. T., Honigmann, A., et al. (2016). Calcium promotes the formation of syntaxin 1 mesoscale domains through phosphatidylinositol 4,5-bisphosphate. Journal of Biological Chemistry, 291(15), 7868-7876. doi:10.1074/jbc.M116.716225.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5262-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-F0EE-A
Genre: Journal Article

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 Creators:
Milovanovic, D.1, Author              
Platen, M., Author
Junius, M., Author
Diederichsen, U., Author
Schaap, I. A. T., Author
Honigmann, A.2, Author              
Jahn, R.1, Author              
van den Bogaar, G., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              

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Free keywords: Calcium; Membrane structure; Plasma membrane; Protein-lipid interaction; SNARE proteins; PI(4; 5)P-2; Clustering; Membrane domains; Syntaxin 1
 Abstract: Phosphatidylinositiol 4,5-bisphosphate (PI(4,5)P2) is a minor component of total plasma membrane lipids, yet it has a substantial role in regulation of many cellular functions including exo- and endocytosis. Recently, it was shown that PI(4,5)P2 and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form domains in the plasma membrane that constitute recognition sites for vesicle docking. Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the molecular mechanism was unknown. Here, using a combination of super-resolution STED microscopy, Foerster resonance energy transfer (FRET) and atomic force microscopy (AFM) we show that calcium ions act as the charge bridges that specifically and reversibly connect multiple syntaxin 1/PI(4,5)P2 complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological calcium concentrations is likely to be important for caaclium-regulated secretion.

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Language(s): eng - English
 Dates: 2016-02-162016-04-08
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M116.716225
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 291 (15) Sequence Number: - Start / End Page: 7868 - 7876 Identifier: -