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Vesicle-associated membrane protein 7

This gene encodes a transmembrane protein that is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. The encoded protein localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: v-SNARE, CAN, Synaptobrevin, VAMP8, VAMP2
Papers on VAMP7
Structure and function of longin SNAREs.
Tareste et al., Paris, France. In J Cell Sci, Jan 2016
Here, we review the first decade of structure-function data on the three prototypical longin SNAREs: Ykt6, VAMP7 and Sec22b.
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
Here, we identified an interaction between VAMP7 and SNAP-47 using a proteomics approach.
Cargo-selective apical exocytosis in epithelial cells is conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3.
Huber et al., Innsbruck, Austria. In J Cell Biol, Dec 2015
Apical exocytosis of NHE3, CFTR (cystic fibrosis transmembrane conductance regulator), and GLUT5 required an interaction cascade of Rab11, Myo5B, Slp4a, Munc18-2, and Vamp7 with Stx3, which cooperate in the final steps of this selective apical traffic pathway.
Leucine-Rich Repeat Kinase 1 Regulates Autophagy through Turning On TBC1D2-Dependent Rab7 Inactivation.
Kumanogoh et al., Suita, Japan. In Mol Cell Biol, Oct 2015
Upon induction of autophagy, LRRK1 was recruited via an association with VAMP7 to the autolysosome, where it activated the Rab7 GTPase-activating protein (GAP) TBC1D2, thereby switching off Rab7 signaling.
STX13 regulates cargo delivery from recycling endosomes during melanosome biogenesis.
Setty et al., Bengaluru, India. In J Cell Sci, Oct 2015
In addition, STX13-dependent cargo transport requires the melanosomal R-SNARE VAMP7, and its silencing blocks the melanosome maturation, reflecting a defect in endosome-melanosome fusion.
Role of tetanus neurotoxin insensitive vesicle-associated membrane protein in membrane domains transport and homeostasis.
Galli et al., Paris, France. In Cell Logist, 2015
Here we show that vesicular SNARE TI-VAMP/VAMP7 plays a major role in membrane domains composition and transport.
Increased gene copy number of VAMP7 disrupts human male urogenital development through altered estrogen action.
Lamb et al., Houston, United States. In Nat Med, 2014
Here we analyzed children born with congenital genitourinary tract masculinization disorders by array-comparative genomic hybridization, which revealed in 1.35% of cases the presence of de novo copy number gains at Xq28 encompassing the VAMP7 gene, which encodes a vesicle-trafficking protein that is part of the SNARE complex.
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).
VAMP7 controls T cell activation by regulating the recruitment and phosphorylation of vesicular Lat at TCR-activation sites.
Hivroz et al., Paris, France. In Nat Immunol, 2013
Here we found, by silencing approaches and genetically modified mice, that the vesicular SNARE VAMP7 was required for the recruitment of Lat-containing vesicles to TCR-activation sites.
Granule exocytosis is required for platelet spreading: differential sorting of α-granules expressing VAMP-7.
Flaumenhaft et al., Boston, United States. In Blood, 2012
These studies identify a new alpha-granule subtype expressing VAMP-7 that moves to the periphery during spreading, supporting the premise that alpha-granules are heterogeneous and demonstrating that granule exocytosis is required for platelet spreading.
Structural basis of the intracellular sorting of the SNARE VAMP7 by the AP3 adaptor complex.
Owen et al., Cambridge, United Kingdom. In Dev Cell, 2012
The binding of VAMP7 to delta-adaptin requires the VAMP7 SNARE motif to be engaged in SNARE complex formation and hence AP3 must transport VAMP7 when VAMP7 is part of a cis-SNARE complex.
Absence of TI-VAMP/Vamp7 leads to increased anxiety in mice.
Galli et al., Paris, France. In J Neurosci, 2012
Behavioral characterization studies indicate that deletion of Vamp7 exon 7 is associated with increased anxiety in mice.
Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration.
Coppolino et al., Guelph, Canada. In J Biol Chem, 2012
The endosomal trafficking and recycling of MT1-MMP was found to be dependent upon Rab7 and VAMP7, and blocking the function of these proteins reduced cell migration and invasion.
v-SNARE composition distinguishes synaptic vesicle pools.
Edwards et al., San Francisco, United States. In Neuron, 2011
VAMP7, and other synaptic vesicle proteins thus target to both recycling and resting pools. However, the proportions differ dramatically, with higher levels of VGLUT1 and VAMP2 in the recycling pool and of VAMP7 in the resting pool
Autophagosome precursor maturation requires homotypic fusion.
Rubinsztein et al., Cambridge, United Kingdom. In Cell, 2011
Atg16L1 precursor homotypic fusion depends on the SNARE protein VAMP7 together with partner SNAREs.
A membrane trafficking pathway regulated by the plant-specific RAB GTPase ARA6.
Ueda et al., Tokyo, Japan. In Nat Cell Biol, 2011
Plants have also evolved a unique repertoire of SNAREs, the most distinctive of which are diverse VAMP7-related longins, including plant-unique VAMP72 derivatives.
Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking.
Galli et al., Paris, France. In Febs Lett, 2010
Here we review the basic properties and functions of the v-SNARE TI-VAMP/VAMP7 (Tetanus neurotoxin insensitive-vesicle associated membrane protein).
The delivery of endocytosed cargo to lysosomes.
Bright et al., Cambridge, United Kingdom. In Biochem Soc Trans, 2009
Heterotypic late endosome-lysosome membrane fusion is mediated by a trans-SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) complex comprising Syntaxin7, Vti1b, Syntaxin8 and VAMP7 (vesicle-associated membrane protein 7).
Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb.
Luzio et al., Cambridge, United Kingdom. In Cell, 2008
Study demonstrates that the clathrin-mediated endocytosis of the SNARE VAMP7 is directly mediated by Hrb, a clathrin adaptor and ArfGAP.
What is the function of neuronal AP-3?
Galli et al., Paris, France. In Biol Cell, 2007
In the present review, we will particularly focus on the recent data concerning the recycling of synaptic vesicles and the function of AP-3 and the v-SNARE (vesicular soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) TI-VAMP (tetanus neurotoxin-insensitive vesicle-associated membrane protein) in these processes.
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