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Vesicle-associated membrane protein 4

VAMP4, vesicle-associated membrane protein 4
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. This protein may play a role in trans-Golgi network-to-endosome transport. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: VAMP7, Insulin, VAMP2, SNAP-23, CAN
Papers using VAMP4 antibodies
Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
Lev Sima et al., In The Journal of Cell Biology, 2004
... Polyclonal anti-VAMP4 and anti-Vti1a antibodies were purchased from Synaptic Systems and from Proteintech Group, ...
Papers on VAMP4
VAMP4 Is an Essential Cargo Molecule for Activity-Dependent Bulk Endocytosis.
Cousin et al., Edinburgh, United Kingdom. In Neuron, Jan 2016
The retrieval of only one reporter, VAMP4-pHluorin, was perturbed by inhibiting ADBE.
The Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).
Proux-Gillardeaux et al., Paris, France. In J Biol Chem, Dec 2015
SNAP-47 preferentially interacted with the trans-Golgi network VAMP4 and post-Golgi VAMP7 and -8.
Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transport.
Kinoshita et al., Ōsaka, Japan. In Mol Biol Cell, Oct 2015
Overexpression of VAMP4, v-SNARE, in VPS54-KO cells partially restored not only endosome-to-TGN retrograde transport, but also anterograde transport of both GPI-anchored and transmembrane proteins.
mVps45 knockdown selectively modulates VAMP expression in 3T3-L1 adipocytes.
Gould et al., York, United Kingdom. In Commun Integr Biol, May 2015
Co-immunoprecipitation experiments in 3T3-L1 adipocytes revealed an interaction between Syntaxin 16 and only VAMP4.
Polarized sorting of the copper transporter ATP7B in neurons mediated by recognition of a dileucine signal by AP-1.
Bonifacino et al., Bethesda, United States. In Mol Biol Cell, Feb 2015
Here we report that polarized sorting of the Cu(2+) transporter ATP7B and the vesicle-SNARE VAMP4 to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the σ1 subunit of the clathrin adaptor AP-1.
Association between DNA methylation and multidrug resistance in human glioma SHG-44 cells.
Wang et al., Chongqing, China. In Mol Med Report, 2015
Genes including SNAP47, VAMP4 and VAMP3 may serve as the downstream effectors of Pgp, COX-2 or PKCα; however, further experiments are required to verify these observations.
Neurite outgrowth induced by NGF or L1CAM via activation of the TrkA receptor is sustained also by the exocytosis of enlargeosomes.
Meldolesi et al., Milano, Italy. In Proc Natl Acad Sci U S A, 2014
Working with wild-type PC12 (wtPC12), a cell model widely used to investigate NGF-induced neurite outgrowth, we found that a few hours of treatment with the neurotrophin (and to a lower extent with basic FGF and EGF) induces the appearance of enlargeosome vesicles competent for VAMP4-dependent exocytosis abundant in high REST-PC12 clones.
Liver-restricted Repin1 deficiency improves whole-body insulin sensitivity, alters lipid metabolism, and causes secondary changes in adipose tissue in mice.
Klöting et al., Leipzig, Germany. In Diabetes, 2014
Repin1 deficiency causes significant changes in potential downstream target molecules including Cd36, Pparγ, Glut2 protein, Akt phosphorylation, and lipocalin2, Vamp4, and Snap23 mRNA expression.
Reelin mobilizes a VAMP7-dependent synaptic vesicle pool and selectively augments spontaneous neurotransmission.
Kavalali et al., Dallas, United States. In Neuron, 2013
The specificity of Reelin action on spontaneous neurotransmitter release is encoded at the level of vesicular SNARE machinery as it requires VAMP7 and SNAP-25 but not synaptobrevin2, VAMP4, or vti1a.
Plin2 inhibits cellular glucose uptake through interactions with SNAP23, a SNARE complex protein.
Atshaves et al., East Lansing, United States. In Plos One, 2012
Expression of the SNARE protein SNAP23 was increased 1.6-fold while levels of syntaxin-5 were decreased 1.7-fold in Plin2 overexpression cells with no significant changes observed in lipid droplet associated proteins Plin1 or FSP27 or with the insulin receptor, GLUT1, or VAMP4.
VAMP4 directs synaptic vesicles to a pool that selectively maintains asynchronous neurotransmission.
Kavalali et al., Dallas, United States. In Nat Neurosci, 2012
The findings of this study suggested that VAMP4 and syb2 diverge functionally, traffic independently and support distinct forms of neurotransmission
VAMP4- and VAMP7-expressing vesicles are both required for cytotoxic granule exocytosis in NK cells.
Strominger et al., Cambridge, United States. In Eur J Immunol, 2011
VAMP7 is involved in many fusion processes and thus plays a more general function in NK-cell activity than VAMP4.
The formation of lipid droplets: possible role in the development of insulin resistance/type 2 diabetes.
Boström et al., Göteborg, Sweden. In Prostaglandins Leukot Essent Fatty Acids, 2011
The fusion is catalyzed by the SNARE proteins SNAP23, syntaxin-5 and VAMP4.
The assembly of lipid droplets and its relation to cellular insulin sensitivity.
Olofsson et al., Göteborg, Sweden. In Biochem Soc Trans, 2009
Lipid droplets grow in size by fusion, which is dependent on dynein and the transfer on microtubules, and is catalysed by the SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins SNAP-23 (23 kDa synaptosome-associated protein), syntaxin-5 and VAMP-4 (vesicle-associated protein 4).
Coiled-coil interactions are required for post-Golgi R-SNARE trafficking.
Peden et al., Cambridge, United Kingdom. In Embo Rep, 2009
Here, we show that the distribution and internalization of VAMPs 3 and 8 are determined solely through a new conserved mechanism that uses coiled-coil interactions, and that VAMP4 does not require these interactions for its trafficking.
The regulated exocytosis of enlargeosomes is mediated by a SNARE machinery that includes VAMP4.
Meldolesi et al., Milano, Italy. In J Cell Sci, 2008
Data show that VAMP4, an R-SNARE that has never been shown to participate in regulated exocytoses, appears to be harboured in the membrane of enlargeosomes and to be a member of the machinery mediating their regulated exocytosis.
SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity.
Olofsson et al., Göteborg, Sweden. In Nat Cell Biol, 2007
Here, we show that lipid droplets are associated with proteins involved in fusion processes in the cell: NSF (N-ethylmaleimide-sensitive-factor), alpha-SNAP (soluble NSF attachment protein) and the SNAREs (SNAP receptors), SNAP23 (synaptosomal-associated protein of 23 kDa), syntaxin-5 and VAMP4 (vesicle-associated membrane protein 4).
The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network.
Hong et al., Singapore, Singapore. In J Biol Chem, 2003
The cytoplasmic domain of this protein is responsible for its correct subcellular targeting, the N-terminal extension contains a dominant autonomous targeting signal for the trans-golgi network
Biosynthesis and secretion of pituitary hormones: dynamics and regulation.
Machen et al., Berkeley, United States. In Arch Physiol Biochem, 2002
Two SNAREs, VAMP4 and synaptotagmin IV, enter newly formed granules but are removed from the maturing granule membrane by vesicle budding.
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