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Vesicle-associated membrane protein 8

This gene encodes an integral membrane protein that belongs to the synaptobrevin/vesicle-associated membrane protein subfamily of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). The encoded protein is involved in the fusion of synaptic vesicles with the presynaptic membrane.[provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: SNAP-23, v-SNARE, VAMP2, Vesicle-Associated Membrane Protein 3, VAMP7
Papers using VAMP8 antibodies
Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
Simon Sanford M. et al., In The Journal of Cell Biology, 1998
... The plasmids were constructed by inserting the mouse VAMP7 or VAMP8 cDNAs followed by a sequence encoding 3× SGG amino acids into the HindII-AgeI site of the CLONTECH pCFP-N1 vector (CLONTECH Laboratories, ...
Papers on VAMP8
Munc13-4 interacts with syntaxin 7, regulates late endosomal maturation, endosomal signaling and TLR9-initiated cellular responses.
Catz et al., San Diego, United States. In Mol Biol Cell, Jan 2016
Here, we identify a novel mechanism of late endosomal maturation that involves a new molecular interaction between the tethering factor Munc13-4, syntaxin 7 and VAMP8.
Chorein Sensitive Dopamine Release from Pheochromocytoma (PC12) Cells.
Lang et al., Bingen am Rhein, Germany. In Neurosignals, Jan 2016
In blood platelets chorein deficiency has been shown to compromise expression of vesicle-associated membrane protein 8 (VAMP8) and thus degranulation.
ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes.
Zhong et al., Stanford, United States. In Nature, May 2015
Here we report that ATG14 (also known as beclin-1-associated autophagy-related key regulator (Barkor) or ATG14L), an essential autophagy-specific regulator of the class III phosphatidylinositol 3-kinase complex, promotes membrane tethering of protein-free liposomes, and enhances hemifusion and full fusion of proteoliposomes reconstituted with the target (t)-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) syntaxin 17 (STX17) and SNAP29, and the vesicle (v)-SNARE VAMP8 (vesicle-associated membrane protein 8).
Impairment of autophagosome-lysosome fusion in the buff mutant mice with the VPS33A(D251E) mutation.
Li et al., Beijing, China. In Autophagy, 2014
The direct association of mutant VPS33A(D251E) with the autophagic SNARE complex, STX17 (syntaxin 17)-VAMP8-SNAP29, was enhanced.
No association of VAMP8 gene polymorphisms with glioma in a Chinese Han population.
Sun et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
Vesicle-associated membrane protein 8 (VAMP8) gene plays an important role in biological functions like endosomal fusion, sequential granule-to-granule fusion and autophagy.
Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes.
Kumar et al., Hattiesburg, United States. In Plos One, 2014
We report the identification of at least six distinct trans-SNARE complexes under enhanced tethering conditions: i) VAMP2/syntaxin3/SNAP-23, ii) VAMP2/syntaxin4/SNAP-23, iii) VAMP3/syntaxin3/SNAP-23, iv) VAMP3/syntaxin4/SNAP-23, v) VAMP8/syntaxin3/SNAP-23, and vi) VAMP8/syntaxin4/SNAP-23.
TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation.
Blander et al., New York City, United States. In Cell, 2014
Instead, MHC-I are recruited from an endosomal recycling compartment (ERC), which is marked by Rab11a, VAMP3/cellubrevin, and VAMP8/endobrevin and holds large reserves of MHC-I.
Ca²⁺-regulated secretory granule exocytosis in pancreatic and parotid acinar cells.
Groblewski et al., Madison, United States. In Cell Calcium, 2014
Studies indicate the early phase is triggered by Ca(2+) and involves the SG proteins VAMP2 (vesicle associated membrane protein2), Ca(2+)-sensing protein synatotagmin 1 (syt1) and the accessory protein complexin 2. The molecular details for regulation of VAMP8-mediated SG exocytosis and the prolonged phase of secretion are still emerging.
Evolutionarily conserved role and physiological relevance of a STX17/Syx17 (syntaxin 17)-containing SNARE complex in autophagosome fusion with endosomes and lysosomes.
Juhász et al., Budapest, Hungary. In Autophagy, 2013
Two recent papers conclude that STX17/syntaxin 17 (Syx17 in Drosophila) has an evolutionarily conserved role in autophagosome fusion with endosomes and lysosomes, acting in one SNARE complex with SNAP29 (ubisnap in Drosophila) and the endosomal/lysosomal VAMP8 (CG1599/Vamp7 in Drosophila).
The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes.
Mizushima et al., Tokyo, Japan. In Cell, 2013
Stx17 interacts with SNAP-29 and the endosomal/lysosomal SNARE VAMP8.
Regulated mucin secretion from airway epithelial cells.
Dickey et al., Raleigh, United States. In Front Endocrinol (lausanne), 2012
The core exocytic machinery is comprised of the SNARE proteins VAMP8, SNAP23, and an unknown Syntaxin protein, together with the scaffolding protein Munc18b.
Dual role of VAMP8 in regulating insulin exocytosis and islet β cell growth.
Gaisano et al., Toronto, Canada. In Cell Metab, 2012
We employed SNARE protein VAMP8-null mice to demonstrate that VAMP8 mediates insulin granule recruitment to the plasma membrane, which partly accounts for GLP-1 potentiation of glucose-stimulated insulin secretion.
VAMP8/endobrevin is a critical factor for the homotypic granule growth in pancreatic acinar cells.
Amihai et al., Tel Aviv-Yafo, Israel. In Cell Tissue Res, 2012
VAMP8 knockout mice were used to show that the SNARE machinery plays a critical role in the process of granule homotypic fusion.
VAMP8 is a vesicle SNARE that regulates mucin secretion in airway goblet cells.
Kreda et al., Chapel Hill, United States. In J Physiol, 2012
VAMP8 regulates mucin granule exocytosis in airway goblet cells, and reduction of its expression may provide a novel therapeutic target to ameliorate airway mucus obstruction in lung diseases
KIF6, LPA, TAS2R50, and VAMP8 genetic variation, low density lipoprotein cholesterol lowering response to pravastatin, and heart disease risk reduction in the elderly.
Schaefer et al., Boston, United States. In Atherosclerosis, 2012
Assessment of KIF6 genotype is not useful in predicting low density lipoprotein cholesterol lowering response to pravastatin, and heart disease risk reduction in the elderly.
The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM.
Owen et al., Cambridge, United Kingdom. In Cell, 2011
Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4,5P(2)-binding, endocytic clathrin adaptor CALM/PICALM.
Vesicle-associated membrane protein 8 (VAMP8) is a SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) selectively required for sequential granule-to-granule fusion.
Thorn et al., Australia. In J Biol Chem, 2011
that granule-to-granule fusion is regulated by VAMP8 containing SNARE complexes distinct from those that regulate primary granule fusion.
Endocytic membrane fusion and buckling-induced microtubule severing mediate cell abscission.
Prekeris et al., Aurora, United States. In J Cell Sci, 2011
Dynamics of FIP3- and VAMP8-containing endosomes reflect the progressive stages of abscission.
The cystic fibrosis transmembrane conductance regulator's expanding SNARE interactome.
Lee et al., Singapore, Singapore. In Traffic, 2011
Members of the STX8/STX7/vesicle transport through interaction with t-SNAREs homolog 1b/VAMP8 SNARE complex, which function in early to late endosome/lysosome traffic, are all known to interact with CFTR.
The delivery of endocytosed cargo to lysosomes.
Bright et al., Cambridge, United Kingdom. In Biochem Soc Trans, 2009
This differs from the trans-SNARE complex required for homotypic late endosome fusion in which VAMP8 replaces VAMP7.
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