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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Vesicle transport through interaction with t-SNAREs homolog 1B

v-SNARE, vti1b, a v-SNARE
Top mentioned proteins: CAN, Synaptobrevin, VAMP2, SNAP-25, NSF
Papers using v-SNARE antibodies
Subcompartments of the macrophage recycling endosome direct the differential secretion of IL-6 and TNFα
Stow Jennifer L. et al., In The Journal of Cell Biology, 2003
... and rat monoclonal anti–mouse TNFα antibodies (Calbiochem and Auspep, respectively), monoclonal antibodies to Stx6 and Vti1b (Translabs; BD Biosciences), monoclonal antibody to TfnR ...
Papers on v-SNARE
The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory protein and confers differential cargo sorting.
Conibear et al., Vancouver, Canada. In Mol Biol Cell, Jan 2016
Loss of Apm2, but not Apm1, increases cell surface levels of the v-SNARE Snc1.
Lipid-anchored synaptobrevin provides little or no support for exocytosis or liposome fusion.
Jackson et al., United States. In J Biol Chem, Jan 2016
To test the role of membrane attachment we generated four variants of the synaptic v-SNARE synaptobrevin-2 (syb2) anchored to the membrane by lipid instead of protein.
The Rab GTPase Rab8 as a shared regulator of ciliogenesis and immune synapse assembly: from a conserved pathway to diverse cellular structures.
Baldari et al., Siena, Italy. In Small Gtpases, Dec 2015
By interacting with the v-SNARE VAMP-3, Rab8 is indeed responsible for the final docking/fusion step in T cell receptor (TCR) recycling to the immune synapse.
'Porosome' discovered nearly 20 years ago provides molecular insights into the kiss-and-run mechanism of cell secretion.
Jena, Detroit, United States. In J Cell Mol Med, Jul 2015
Elucidation of the porosome structure, its chemical composition and functional reconstitution into artificial lipid membrane, and the molecular assembly of membrane-associated t-SNARE and v-SNARE proteins in a ring or rosette complex resulting in the establishment of membrane continuity to form a fusion pore at the porosome base, has been demonstrated.
The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.
Shen et al., Boulder, United States. In Nat Commun, 2014
Here we first demonstrate that two mutations in the vesicle-anchored v-SNARE selectively impair the ability of Munc18-1 to promote trans-SNARE zippering, whereas other known Munc18-1/SNARE-binding modes are unaffected.
Characterization of VAMP2 in Schistosoma japonicum and the Evaluation of Protective Efficacy Induced by Recombinant SjVAMP2 in Mice.
Lin et al., Shanghai, China. In Plos One, 2014
SjVAMP2 is a member of the synaptobrevin superfamily harboring the v-SNARE coiled-coil homology domain.
Docking of lytic granules at the immunological synapse in human CTL requires Vti1b-dependent pairing with CD3 endosomes.
Hoth et al., Homburg, Germany. In J Immunol, 2011
Vti1b-dependent tethering of Lytic granule and CD3-endo determines accumulation, docking, and efficient lytic granule secretion at the immunological synapse.
A role for V-ATPase subunits in synaptic vesicle fusion?
Seagar et al., Marseille, France. In J Neurochem, 2011
A synaptic vesicle v-SNARE protein (VAMP2 or synaptobrevin), in association with two plasma membrane t-SNAREs (syntaxin 1 and SNAP25), assemble to form a protein complex that is largely accepted as the minimal membrane fusion machine.
[The role of docosahexaenoic acid in neuronal function].
Zgórzyńska et al., Łódź, Poland. In Postepy Hig Med Dosw (online), 2010
DHA present in membrane phospholipids facilitates v-SNARE/t-SNARE complex formation, which is necessary for fusion of synaptic vesicles and plasma membranes necessary for transmitter exocytosis, and neurite outgrowth-dependent plasticity.
Role of SNAREs in membrane fusion.
Jena, Detroit, United States. In Adv Exp Med Biol, 2010
For example in cell secretion, target membrane proteins at the cell plasma membrane SNAP-25 and syntaxin termed t-SNAREs, and secretory vesicle-associated protein VAMP or v-SNARE, are part of the conserved protein complex involved in fusion of opposing membranes.
Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes.
Amano et al., Suita, Japan. In Mol Biol Cell, 2010
Results suggest that the combinational SNARE proteins VAMP8 and Vti1b mediate the fusion of antimicrobial and canonical autophagosomes with lysosomes, an essential event for autophagic degradation.
Complexin controls the force transfer from SNARE complexes to membranes in fusion.
Südhof et al., Dallas, United States. In Science, 2009
Consistent with this hypothesis, a mutation in the membrane insertion sequence of the v-SNARE synaptobrevin/vesicle-associated membrane protein (VAMP) phenocopied the complexin loss-of-function state without impairing complexin binding to SNARE complexes.
Endosomal SNARE proteins regulate CFTR activity and trafficking in epithelial cells.
Thoreau et al., Poitiers, France. In Exp Cell Res, 2008
Results report that syntaxin 7, syntaxin 8, vti1b and VAMP8 physically and functionally interact with CFTR.
v-SNARE actions during Ca(2+)-triggered exocytosis.
Bruns et al., Homburg, Germany. In Cell, 2007
These observations provide evidence that v-SNARE proteins drive Ca(2+)-triggered membrane fusion at millisecond time scale and support a model wherein continuous molecular pulling by SNAREs guides the vesicle throughout the consecutive stages of exocytosis.
Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission.
Doxsey et al., Worcester, United States. In Cell, 2005
Exocyst disruption induces accumulation of v-SNARE-containing vesicles at the midbody ring.
EpsinR is an adaptor for the SNARE protein Vti1b.
Robinson et al., Cambridge, United Kingdom. In Mol Biol Cell, 2004
epsin 4 epsin-related protein is an adaptor for vti1b
Mutual control of membrane fission and fusion proteins.
Mayer et al., Lausanne, Switzerland. In Cell, 2004
This activity is independent of the SNARE coactivator Sec17p/alpha-SNAP and of the v-SNARE.
Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes.
Bean et al., Houston, United States. In J Biol Chem, 2004
Ca(2+) dissociates the Hrs-containing complex but not the VAMP-2-containing SNARE complex
Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles.
Schekman et al., Berkeley, United States. In Cell, 2003
We identified a site on Sec24p that recognizes the v-SNARE Bet1p and show that packaging of a number of cargo molecules is disrupted when mutations are introduced at this site.
TRP Channel Trafficking
Ferrer-Montiel et al., Boca Raton, United States. In Unknown Journal, 0001
For instance, the interaction of the vesicle membrane SNARE (v-SNARE) synaptobrevin 2, and the corresponding SNAREs in the target membrane (t-SNAREs), syntaxin 1 and SNAP25, results in the formation of a remarkably stable ternary complex that ensures the docking and fusion of vesicles at the active zone upon receiving the stimulus, normally an increase in the intracellular concentration of Ca(2+) ([Ca [2]]i).(+5)
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