Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8302015 | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | 2015 | 9 Pages |
Abstract
PI(4,5)P2 participates directly in priming and possibly in fusion steps of Ca2Â +-triggered vesicle exocytosis. High concentration nanodomains of PI(4,5)P2 reside on the plasma membrane of neuroendocrine cells. A subset of vesicles that co-localize with PI(4,5)P2 domains appear to undergo preferential exocytosis in stimulated cells. PI(4,5)P2 directly regulates vesicle exocytosis by recruiting and activating PI(4,5)P2-binding proteins that regulate SNARE protein function including CAPS, Munc13-1/2, synaptotagmin-1, and other C2 domain-containing proteins. These PI(4,5)P2 effector proteins are coincidence detectors that engage in multiple interactions at vesicle exocytic sites. The SNARE protein syntaxin-1 also binds to PI(4,5)P2, which promotes clustering, but an activating role for PI(4,5)P2 in syntaxin-1 function remains to be fully characterized. Similar principles underlie polarized constitutive vesicle fusion mediated in part by the PI(4,5)P2-binding subunits of the exocyst complex (Sec3, Exo70). Overall, focal vesicle exocytosis occurs at sites landmarked by PI(4,5)P2, which serves to recruit and/or activate multifunctional PI(4,5)P2-binding proteins. This article is part of a Special Issue entitled Phosphoinositides.
Keywords
FWHMPLCMunc13SNAREMARCKSPKCTIRFVesicle exocytosisPI(4)PPI(4,5)P2myristoylated alanine-rich C kinase substrateSynaptotagminfull width half maximumPhosphatidylinositol(4,5)bisphosphatephosphatidylinositol 4-monophosphatephosphatidylinositol 4,5-bisphosphatephospholipase CTotal internal reflectance fluorescenceSTEDstimulated emission depletion microscopyPhotoactivated localization microscopyPalmSNARE proteinProtein kinase Csoluble N-ethylmaleimide-sensitive factor attachment protein receptor
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Thomas F.J. Martin,