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Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P(2) and syntaxin 1, a SNARE protein that catalyzes...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4824995/ https://www.ncbi.nlm.nih.gov/pubmed/26884341 http://dx.doi.org/10.1074/jbc.M116.716225 |
Sumario: | Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P(2) 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 superresolution stimulated emission depletion microscopy, FRET, and atomic force microscopy, we show that Ca(2+) acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/PI(4,5)P(2) complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological Ca(2+) concentrations is likely to be important for Ca(2+)-regulated secretion. |
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