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HighlightsSNAREs are membrane-anchored proteins that usually contain a C-terminal transmembrane domain, an adjacent SNARE motif, and an N-terminal domain. They are key regulators in all fusion events. Before fusion, the SNARE motifs assemble into a four-helix bundle. There are four different conserved SNARE motifs: Qa-, Qb-, Qc-, and R-SNAREs. Vesicle docking and fusion requires a specific R-SNARE on the vesicle to bind to the Q-SNAREs to form a trans-complex, thus pulling the membranes in close proximity and facilitating fusion. Different intracellular fusion events involve SNARE complexes of different composition. VTI1B is a 232-amino-acid protein that in humans is encoded by the VTI1B gene. It is a Qb SNARE motif that can form a complex with other SNARE proteins such as syntaxin 11 (Stx11). VTI1B is localized to the early and late endosomes, the Golgi, and trans-Golgi network.
| Basic Information of VTI1B | |
| Protein Name | Vesicle transport through interaction with t-SNAREs homolog 1B |
| Gene Name | VTI1B |
| Aliases | Vesicle transport v-SNARE protein Vti1-like 1, Vti1-rp1 |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q9UEU0 |
| Transmembrane Times | 1 |
| Length (aa) | 232 |
| Sequence | MASSAASSEHFEKLHEIFRGLHEDLQGVPERLLGTAGTEEKKKLIRDFDEKQQEANETLAEMEEELRYAPLSFRNPMMSKLRNYRKDLAKLHREVRSTPLTATPGGRGDMKYGIYAVENEHMNRLQSQRAMLLQGTESLNRATQSIERSHRIATETDQIGSEIIEELGEQRDQLERTKSRLVNTSENLSKSRKILRSMSRKVTTNKLLLSIIILLELAILGGLVYYKFFRSH |
VTI1B functions in a number of different trafficking pathways. Firstly, VTI1B is involved in autophagy. VTI1B forms a complex with syntaxin 11 (STX7), syntaxin 8 (STX8), and VAMP7, thereby mediating the fusion between recycling endosomes and autophagosomes. Moreover, by forming a complex with STX and VAMP3, VTI1B functions in GAS-containing autophagosome-like vacuole (GcAV)-recycling endosome (RE) fusion. Secondly, it is necessary for the post-Golgi trafficking of cytokines in macrophages. In cytotoxic lymphocytes, it is required for the release of secretory lysosomes. Additionally, VTI1B may be concerned with increased secretion of cytokines associated with cellular senescence.
This study identified the SNARE complex that was involved in recycling endosome (RE)-autophagosome fusion during Group A Streptococcus (GAS) infection, especially the subcellular localization of STX-family proteins. The results showed that STX6 formed a complex with VTI1B and VAMP3 to regulate GcAV-RE fusion.
Using both Vti1a and Vti1b-deficient mice, this study demonstrated that lack of these tow SNARE motifs led to major axon tracts and massive neurodegeneration.
This study reported that syntaxin 11 (Stx 11) can regulate the availability of Vti1b and it bound to Vti1b to regulate trafficking steps between late endosomes, lysosomes, and the cell surface in macrophages.
Using a combination of bioinformatic approaches, qRT-PCR, immunoblotting, and confocal microscopy, this study characterized the Vti family of SNARE proteins in A. maculatum and A. americanum salivary glands.
This study provided evidence that epsinR, a clathrin-coated vesicle-associated protein, was an adaptor for viti1b.
We constantly strive to provide unparalleled membrane preparation services using a variety of strategies provided by our powerful Magic™ Membrane Protein Production Platform. These include the use of detergent micelles, liposomes, nanodiscs, and polymers. We pursue to tailor the strategies specific to your proteins in order to maximally keep their structural and functional integrity. Besides, we can also provide customized anti-VTI1B antibody development services based on our cutting-edge Magic™ anti-membrane protein antibody discovery platform.
Contact us if are interested in our membrane protein preparation services.
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