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SNARE-dependent exocytosis

Gasnier B (2000) The loading of neurotransmitters into synaptic vesicle. Biochimie 82 327-37 Giraudo CG, Eng WS, Melia TJ, Rothman JE (2006) A clamping mechanism involved in SNARE-dependent exocytosis. Science 313 676-80... [Pg.22]

Vennekens R, Olausson J, Meissner M, Bloch W, Mathar I, Philipp SE, Schmitz F, Weissgerber R Nilius B, Flockerzi V, Freichel M Increased IgE-dependent mast cell activation and anaphylactic responses in mice lacking the calcium-activated nonselective cation channel XRPM4. Nat Immunol 2007 8 312-320. Guo Z, Xurner C, Castle D Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Cell 1998 94 537-548. [Pg.64]

Fig. 5 GPCR regulation of exocytosis downstream of Ca2+-entry. (a) Sequence of steps leading from recruitment to maturation of synaptic vesicles from a reserve pool (RP) to a readily-releasable pool (RRP) displaying slow (asynchronous) and fast (synchronous highly Ca2+-sensitive pool, HCSP synaptotagmin 1 (SYT 1) supported) components, (b) Protein-protein interactions of SNARES (SYX, syntaxin SYB, synaptobrevin and SNAP-2s-7S complex) and major putative regulatory proteins. Phosphoproteins are shown in shaded boxes (phosphorylation sites for PKA and PKC are indicated where known) with phosphorylation-dependent interactions depicted by arrows (increase indicated by filled arrows decrease indicated by open arrows). Circle-end connectors indicate a phosphorylation-independent or as yet unspecified interaction. Potential effects of interactions at various points of the sequence in A are discussed in the text. Fig. 5 GPCR regulation of exocytosis downstream of Ca2+-entry. (a) Sequence of steps leading from recruitment to maturation of synaptic vesicles from a reserve pool (RP) to a readily-releasable pool (RRP) displaying slow (asynchronous) and fast (synchronous highly Ca2+-sensitive pool, HCSP synaptotagmin 1 (SYT 1) supported) components, (b) Protein-protein interactions of SNARES (SYX, syntaxin SYB, synaptobrevin and SNAP-2s-7S complex) and major putative regulatory proteins. Phosphoproteins are shown in shaded boxes (phosphorylation sites for PKA and PKC are indicated where known) with phosphorylation-dependent interactions depicted by arrows (increase indicated by filled arrows decrease indicated by open arrows). Circle-end connectors indicate a phosphorylation-independent or as yet unspecified interaction. Potential effects of interactions at various points of the sequence in A are discussed in the text.
B50 (GAP-43) phosphorylation by PKC uncouples the inhibitory tone imposed by stimulation of Ga0, (Misonou et al. 1998 Ohara-Imaizumi et al. 1992), and, in so doing, effects facilitation of exocytosis. Interestingly in this regard, B50 (GAP-43) has been shown to interact with components of the SNARE complex in a PKC phosphorylation-dependent manner (Haruta et al. 1997). [Pg.237]

Blackmer T, Larsen EC, Bartleson C et al (2005) G protein betagamma directly regulates SNARE protein fusion machinery for secretory granule exocytosis. Nat Neurosci 8 421-5 Boczan J, Leenders AG, Sheng ZH (2004) Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis. J Biol Chem 279 18911-19... [Pg.244]


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See also in sourсe #XX -- [ Pg.351 ]




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