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.; Jahn, R.; van den Bogaar, G.

doi:10.1074/jbc.M116.716225

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

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Milovanovic, D.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Honigmann, A.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Jahn, R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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http://www.jbc.org/content/291/15/7868.full?sid=6dc53221-c57e-4b55-a32f-ed57f175cf55
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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-5262-8

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.