ArticleThe Journal of biological chemistry2013
The function of vacuolar ATPase (V-ATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 97 citations in OpenAlex.
- Peripheral blood CD14 + monocytes in luminal breast carcinoma subtypes: in preliminary research and overview of candidate biomarker proteins.Scientific reports · 2026Article
- Maturation stage-specific V-ATPase disassembly explains the neutral pH of mature mucocyst lysosome-related organelles in Tetrahymena thermophila.Journal of cell science · 2025Article
- Deacidification of the Endolysosomal System by the Vesicular Proton Pump V-ATPase Inhibitor Bafilomycin A1 Affects EGF Receptor Endocytosis Differently in Endometrial MSC and HeLa Cells.International journal of molecular sciences · 2025Article
- Monoclonal nanobodies alter the activity and assembly of the yeast vacuolar HbioRxiv : the preprint server for biology · 2025Article
- Clinical Proteomics Reveals Vulnerabilities in Noninvasive Breast Ductal Carcinoma and Drives Personalized Treatment Strategies.Cancer research communications · 2025Article
- Integrated thermal proteome and thermal proximity co-aggregation profiling identifies ATP6V1C1 as a novel anti-cancer drug target.International journal of biological sciences · 2025Article
- The different roles of V-ATPase a subunits in phagocytosis/endocytosis and autophagy.Autophagy · 2024Article
- A nanobody against the V-ATPase c subunit inhibits metastasis of 4T1-12B breast tumor cells to lung in mice.Oncotarget · 2024Article
- The PMA phorbol ester tumor promoter increases canonical Wnt signaling via macropinocytosis.eLife · 2023Article
- Identification of ATP6V0A4 as a potential biomarker in renal cell carcinoma using integrated bioinformatics analysis.Oncology letters · 2023Article
- Characterization of a PIP Binding Site in the N-Terminal Domain of V-ATPase a4 and Its Role in Plasma Membrane Association.International journal of molecular sciences · 2023Article
- The cytosolic N-terminal domain of V-ATPase a-subunits is a regulatory hub targeted by multiple signals.Frontiers in molecular biosciences · 2023Review
- The V-ATPases in cancer and cell death.Cancer gene therapy · 2022Review
- Review
- Detection and quantification of the vacuolar H+ATPase using the Legionella effector protein SidK.The Journal of cell biology · 2022Article
- Role of pH Regulatory Proteins and Dysregulation of pH in Prostate Cancer.Reviews of physiology, biochemistry and pharmacology · 2022Article
- Ion Channels, Transporters, and Sensors Interact with the Acidic Tumor Microenvironment to Modify Cancer Progression.Reviews of physiology, biochemistry and pharmacology · 2022Review
- The V-ATPaseInternational journal of molecular sciences · 2021Review
- The HAmerican journal of physiology. Cell physiology · 2021Review
- Role of the V1G1 subunit of V-ATPase in breast cancer cell migration.Scientific reports · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The vacuolar H(+) ATPases (V-ATPases) are ATP-driven proton pumps that transport protons across both intracellular and plasma membranes. Previous studies have implicated V-ATPases in the invasiveness of various cancer cell lines. In this study, we evaluated the role of V-ATPases in the invasiveness of two closely matched human breast cancer lines. MCF10a cells are a non-invasive, immortalized breast epithelial cell line, and MCF10CA1a cells are a highly invasive, H-Ras-transformed derivative of MCF10a cells selected for their metastatic potential. Using an in vitro Matrigel assay, MCF10CA1a cells showed a much higher invasion than the parental MCF10a cells. Moreover, this increased invasion was completely sensitive to the specific V-ATPase inhibitor concanamycin. MCF10CA1a cells expressed much higher levels of both a1 and a3 subunit isoforms relative to the parental line. Isoforms of subunit a are responsible for subcellular localization of V-ATPases, with a3 and a4 targeting V-ATPases to the plasma membrane of specialized cells. Knockdown of either a3 alone or a3 and a4 together using isoform-specific siRNAs inhibited invasion by MCF10CA1a cells. Importantly, overexpression of a3 but not the other a subunit isoforms greatly increased the invasiveness of the parental MCF10a cells. Similarly, overexpression of a3 significantly increased expression of V-ATPases at the plasma membrane. These studies suggest that breast tumor cells employ particular a subunit isoforms to target V-ATPases to the plasma membrane, where they function in tumor cell invasion.
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