VTI1B Membrane Protein Introduction

Introduction of VTI1B

SNAREs 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

Functions of VTI1B Membrane Protein

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.

VTI1B Membrane Protein Introduction

Application of VTI1B Membrane Protein in Literature

Nozawa T., et al. The STX6-VTI1B-VAMP3 complex facilitates xenophagy by regulating the fusion between recycling endosomes and autophagosomes. Autophagy. 2017, 13(1): 57-69. PubMed ID: 27791468

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.
Kunwar A.J., et al. Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development. Proceedings of the National Academy of Sciences. 2011, 108(6):2575-80. PubMed ID: 21262811

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.
Offenhäuser C., et al. Syntaxin 11 binds Vti1b and regulates late endosome to lysosome fusion in macrophages. Traffic. 2011, 12(6): 762-773. PubMed ID: 21388490

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.
Villarreal A.M., et al. Molecular characterization and functional significance of the Vti family of SNARE proteins in tick salivary glands. Insect biochemistry and molecular biology. 2013, 43(5): 483-493. PubMed ID: 23499931

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.
Hirst J., et al. EpsinR is an adaptor for the SNARE protein Vti1b. Molecular biology of the cell. 2004, 15(12): 5593-5602. PubMed ID: 15371541

This study provided evidence that epsinR, a clathrin-coated vesicle-associated protein, was an adaptor for viti1b.

VTI1B Preparation Options

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.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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