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Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Additionally we are shipping VAMP3 Antibodies (80) and VAMP3 Proteins (11) and many more products for this protein.
phosphatidylinositol 4-kinase (show PI4KB ELISA Kits) IIalpha knockdown inhibited vesicle-associated membrane protein 3 trafficking to perinuclear membranes and impaired the rate of VAMP3-mediated recycling of the transferrin receptor
The small GTPase (show RACGAP1 ELISA Kits) Rab8 (show RAB8A ELISA Kits) interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse.
phosphatidylinositol 4-kinase (show PI4KA ELISA Kits) IIalpha knockdown inhibited vesicle-associated membrane protein 3 trafficking to perinuclear membranes and impaired the rate of VAMP3-mediated recycling of the transferrin receptor
highlight the role that VAMP3 and VAMP7 (show VAMP7 ELISA Kits) play in selection of the pathways leading to generation of ultrastructurally different LC3 (show MAP1LC3A ELISA Kits) compartments
Liquid chromatography-MS/MS analysis showed that the HHV-6 gM/gN complex interacts with the v-SNARE (show VTI1B ELISA Kits) protein, vesicle-associated membrane protein 3 (VAMP3).
These results indicated that Uukuniemi virus relies on VAMP3 for penetration, providing an indication of added complexity in the trafficking of viruses through the endocytic network.
Genome-wide expression profiling identified the transcription of ADIPOR1, VAMP3 and C11ORF10 to be correlated with decreased ANRIL expression in a time-dependent manner.
Data suggest VAMP3 and SNAP23 (synaptosomal-associated protein 23 (show SNAP23 ELISA Kits) kDa) participate in interleukin-1beta-, interleukin-1 receptor-, calcium signaling-dependent secretion/exocytosis of interleukin-6 (show IL6 ELISA Kits) and tumor necrosis factor alpha (show TNF ELISA Kits) from synoviocytes.
Data suggest a new integrin trafficking pathway in which endocytosed integrins are transported from VAMP3-containing recycling endosomes to STX6 (show STX6 ELISA Kits)-containing trans-Golgi network before being recycled to the plasma membrane.
mutation of the Godzilla ubiquitylation target lysines on VAMP3 abrogates the formation of enlarged endosomes induced by either Godzilla or RNF167 (show RNF167 ELISA Kits).
Endothelial cells specifically select VAMP 3 over VAMP8 (show VAMP8 ELISA Kits) to cooperate with syntaxin 4 (show STX4 ELISA Kits) and SNAP23 (show SNAP23 ELISA Kits) in the Ca(2 (show CA2 ELISA Kits)+)-triggered fusion of Weibel-Palade bodies with the plasma membrane.
VAMP3 is required for normal NKCC2 (show SLC12A1 ELISA Kits) expression, renal function, and blood pressure.
Although a slight decrease in the rate of recovery of surviving bacteria was observed between 12 h and 36 h post-infection with Brucella melitensis, this was not significant indicating that VAMP3 is not involved in Brucella survival.
Protein kinase D (show PRKD1 ELISA Kits) activates GLUT4 (show SLC2A4 ELISA Kits) translocation via a VAMP3-dependent trafficking step.
This important SNARE (show VTI1B ELISA Kits) complex facilitates macrophage adhesion, spreading, and persistent macrophage migration on fibronectin (show FN1 ELISA Kits) through the delivery of VAMP3-positive membrane with its cargo to expand the plasma membrane.
VAMP3 mediates fusion of recycling endosome-derived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway
Cellubrevin alterations and Mycobacterium tuberculosis phagosome maturation arrest.
SNARE (show VTI1B ELISA Kits) proteins (cellubrevin, syntaxin 4 (show STX4 ELISA Kits)) are involved in late steps of GLUT4 (show SLC2A4 ELISA Kits) translocation in adipocyte differentiation.
The requirement of vamp3 in phagocytosis in macrophages was determined in vamp3 knockout mice
cellubrevin/VAMP-3 is not a requirement for the platelet release reaction in mice.
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
vesicle-associated membrane protein 3
, synaptic vesicle SNARE
, vesicle-associated membrane protein 3 (cellubrevin)