Target intelligence / Profile preview

Vacuolar ATPase subunit B2 (ATP6V1B2)

Target
ATP6V1B2
Molecular classification
Enzyme (proton-translocating ATPase), Transporter (proton pump)
01

Overview

Vacuolar ATPase subunit B2 (ATP6V1B2) is a non-catalytic component of the V1 sector of the V-ATPase complex, a multi-subunit enzyme responsible for acidifying intracellular compartments including lysosomes, endosomes, and synaptic vesicles[1][3]. The V-ATPase is vital for such processes as protein degradation, receptor-mediated endocytosis, neurotransmitter storage, and autophagy. ATP6V1B2 is ubiquitously expressed, with important roles in the brain, osteoclasts, and inner ear. Mutations in ATP6V1B2 can cause syndromic deafness and developmental disorders due to impaired lysosomal acidification and subsequent disruption of cellular degradation pathways, leading to cellular apoptosis, especially in neurons[1][3]. The protein is an established research target for pharmacological inhibition in studies of cell biology and disease, but no clinically approved drugs target this subunit directly.

Other names
V-type proton ATPase subunit B, brain isoformATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2VATB2V-ATPase B2 subunitATP6B2VPP3Vma2HO57Endomembrane proton pump 58 kDa subunitVacuolar proton pump subunit B 2ATP6B1B2DOODZLS2testicular secretory protein Li 65vacuolar H+-ATPase 56,000 subunit
02

Mechanism of action

Inhibition of proton translocation (by V-ATPase inhibitors, preventing ATP-driven proton pumping and organellar acidification)

03

Biological functions

Organelle acidificationProtein sortingZymogen activationReceptor-mediated endocytosisSynaptic vesicle proton gradient generationAutophagy and lysosomal degradationCellular pH regulation
04

Disease associations

Syndromic deafness, including Deafness, Congenital, With Onychodystrophy, Autosomal DominantZimmermann-Laband syndrome 2Lysosomal storage and neurodegenerative disease (through altered lysosomal acidification and autophagy)
05

Safety considerations

Global inhibition may affect essential organelle acidification processes in all cells, producing broad toxicityDisruption affects lysosomal function and autophagy, with impacts on neuronal survival and general cell health[3]
06

Interacting drugs

Bafilomycin A1 (known research inhibitor of V-ATPase, not clinically approved)

1 more in the full profile.

07

Biomarkers

No established FDA-approved biomarkers; loss-of-function mutations in ATP6V1B2 serve as genetic markers for diagnosis of DDOD syndrome and related disorders[3].

Beyond the preview

Go deeper on Vacuolar ATPase subunit B2 (ATP6V1B2).

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Full profile access

Explore the programs pursuing this target and their development progress.

  • Drug candidates
  • Developers
  • Development stage

Clinical trials

Full profile access

Follow the clinical studies evaluating therapies directed at this target.

  • Trial design
  • Status
  • Readouts

Competitive landscape

Full profile access

Compare approaches across drug candidates, modalities, and indications.

  • Programs
  • Modalities
  • Indications

Literature & evidence

Full profile access

Investigate the research and source evidence behind target biology and development.

  • Publications
  • Sources
  • Analysis

Patents

Full profile access

Explore patent activity around therapies and technologies addressing this target.

  • Patents
  • Assignees
  • Technologies

Research & analysis

Full profile access

Connect target biology, drug development, and emerging evidence in your research.

  • Biology
  • Development news
  • Analysis

Bring the full picture into focus.

See how Gosset can support your research on Vacuolar ATPase subunit B2 (ATP6V1B2).

Explore the full profile

Gosset Free

Get started with Gosset.

Enter your work email and we’ll be in touch with next steps.

Work email preferred.

Book a call