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| ATP6V0A2 | |
|---|---|
| Name | ATP6V0A2 |
| Chromosome | 12 |
| Location | 12q13.11 |
| Synonyms | a2 subunit V0, V-ATPase a2 isoform |
ATP6V0A2 ATP6V0A2 encodes the a2 isoform of the V0 sector of the vacuolar-type H+-ATPase, implicated in intracellular acidification and vesicular trafficking in humans, and is studied across cell biology, developmental biology, and medical genetics. Research on ATP6V0A2 intersects with investigations by groups at institutions such as National Institutes of Health, Harvard University, Massachusetts Institute of Technology, Stanford University and clinical reports from centers including Mayo Clinic, Johns Hopkins Hospital, Great Ormond Street Hospital and Mount Sinai Hospital.
ATP6V0A2 contributes to proton translocation by the vacuolar ATPase and thereby regulates pH within organelles such as the Golgi apparatus and endosomes, a role characterized in cell-based studies from laboratories at University of Cambridge, University of Oxford, California Institute of Technology, Max Planck Society and CNRS. Its function affects post-translational modification pathways analyzed in proteomics projects at European Molecular Biology Laboratory, Broad Institute, Wellcome Trust Sanger Institute, Cold Spring Harbor Laboratory and Laboratory of Molecular Biology, altering processes documented in reviews sponsored by World Health Organization and discussed at conferences like the American Society for Cell Biology annual meeting.
ATP6V0A2 is a membrane-integral subunit of the V0 sector comprising multiple transmembrane helices; structural information derives from cryo-electron microscopy and biochemical studies by groups at Max Planck Institute of Biophysics, University of California, San Francisco, Yale University, Princeton University and ETH Zurich. Expression patterns were profiled in datasets from consortia including GTEx, ENCODE Project Consortium, Human Protein Atlas, 1000 Genomes Project and The Cancer Genome Atlas, showing differential expression across tissues reported by clinical centers such as Cleveland Clinic, Karolinska Institutet, University College London, University of Toronto and Seoul National University.
Mutations in ATP6V0A2 are causative for autosomal recessive cutis laxa type 2A and related syndromes, with clinical descriptions published by teams at Baylor College of Medicine, University of California, San Diego, Children's Hospital of Philadelphia, Universität Heidelberg and Sorbonne University. Phenotypes include connective tissue and neurologic manifestations documented in case series from Great Ormond Street Hospital, Hospital for Sick Children (Toronto), Vanderbilt University Medical Center, Royal Free Hospital and Johns Hopkins Hospital and summarized in reviews appearing in journals affiliated with American College of Medical Genetics, European Society of Human Genetics and American Academy of Pediatrics.
Pathogenic variants in ATP6V0A2 disrupt organellar acidification, impair Golgi function and lead to defective glycosylation and extracellular matrix assembly; mechanistic insights were obtained from biochemical experiments at Scripps Research, Roche, Novartis, Pfizer and academic groups at University of Pennsylvania and McGill University. These disruptions connect to cellular stress responses and developmental pathways studied in models introduced by investigators at MIT, Imperial College London, Duke University, University of California, Los Angeles and Weill Cornell Medicine and discussed at symposia organized by American Society for Biochemistry and Molecular Biology and Gordon Research Conferences.
ATP6V0A2 interacts with other V-ATPase subunits and trafficking machinery components identified through proteomics and yeast two-hybrid screens conducted at Stanford University, Broad Institute, European Bioinformatics Institute, Dana-Farber Cancer Institute and Cold Spring Harbor Laboratory. Reported binding partners include regulatory subunits and Rab-family effectors characterized in studies from University of Geneva, University of Copenhagen, Tokyo Institute of Technology, Seoul National University and Australian National University.
Knockout and transgenic models in mouse and zebrafish, developed at facilities such as Jackson Laboratory, European Mouse Mutant Archive, Zebrafish International Resource Center, Wellcome Sanger Institute and RIKEN, have recapitulated aspects of the human phenotype and informed preclinical studies at Novartis Institutes for BioMedical Research, GlaxoSmithKline, AstraZeneca and academic centers including University of Cambridge and Harvard Medical School. Functional studies leveraging CRISPR/Cas9, RNAi and chemical biology approaches were published by consortia and labs affiliated with Broad Institute, Whitehead Institute, Cold Spring Harbor Laboratory, Whitehead Institute for Biomedical Research and the European Molecular Biology Organization.
Category:Genes on human chromosome 12