ArticleProceedings of the National Academy of Sciences of the United States of America2022
Identification of mEAK-7 as a human V-ATPase regulator via cryo-EM data mining.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Inactive ryanodine receptors sustain lysosomal availability for autophagy by promoting ER-lysosomal contact site formation.Nature communications · 2026Article
- ATG16L1 controls mammalian vacuolar proton ATPase.The Journal of cell biology · 2025Article
- Stress granule clearance mediated by V-ATPase-interacting protein NCOA7 mitigates ovarian aging.Nature aging · 2025Article
- Article
- Oxr1 and Ncoa7 regulate V-ATPase to achieve optimal pH for glycosylation within the Golgi apparatus and trans-Golgi network.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025Article
- Human V-ATPase function is positively and negatively regulated by TLDc proteins.Structure (London, England : 1993) · 2024Article
- Neuroinflammation and Lysosomal Abnormalities Characterise the Essential Role for Oxidation Resistance 1 in the Developing and Adult Cerebellum.Antioxidants (Basel, Switzerland) · 2024Article
- Defective Lamtor5 Leads to Autoimmunity by Deregulating v-ATPase and Lysosomal Acidification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Molecular mechanism of Oxr1p mediated disassembly of yeast V-ATPase.EMBO reports · 2024Article
- Targeting of lysosomal-bound protein mEAK-7 for cancer therapy.Frontiers in oncology · 2024Review
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Vacuolar-type adenosine triphosphatases (V-ATPases) not only function as rotary proton pumps in cellular organelles but also serve as signaling hubs. To identify the endogenous binding partners of V-ATPase, we collected a large dataset of human V-ATPases and did extensive classification and focused refinement of human V-ATPases. Unexpectedly, about 17% of particles in state 2 of human V-ATPases display additional density with an overall resolution of 3.3 Å. Structural analysis combined with artificial intelligence modeling enables us to identify this additional density as mEAK-7, a protein involved in mechanistic target of rapamycin (mTOR) signaling in mammals. Our structure shows that mEAK-7 interacts with subunits A, B, D, and E of V-ATPases in state 2. Thus, we propose that mEAK-7 may regulate V-ATPase function through binding to V-ATPases in state 2 as well as mediate mTOR signaling.
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