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A novel, dominant disease mechanism of distal renal tubular acidosis with specific variants in ATP6V1B1.
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Paediatric Nephrology, UZ Leuven and Department of Cellular and Molecular Physiology, KUL, Leuven, Belgium.
Background And Hypothesis: ATP6V1B1 encodes a subunit of the vacuolar H+-ATPase and pathogenic variants are associated with autosomal recessive distal renal tubular acidosis (dRTA) with deafness. Heterozygous variants predicted to affect a specific amino acid, Arg394, have been recurrently reported in dRTA but their significance has been unclear. We hypothesised that these variants are associated with a dominant disease mechanism.
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Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan. Electronic address:
The F domain of FF-ATP synthases/ATPases (FF) possesses three catalytic sites on the three αβ interfaces, termed αβ, αβ, and αβ, located mainly on the β subunits. The enzyme also has three non-catalytic ATP-binding sites on the three αβ interfaces, located mainly on the α subunits. When ATP does not bind to the non-catalytic site, FF becomes significantly prone to ADP inhibition, ultimately resulting in the loss of ATPase activity.
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Plant plasma membrane (PM) H-ATPase functions as a proton-motive force by exporting cellular protons to establish a transmembrane chemical gradient of H ions and an accompanying electrical gradient. These gradients are crucial for plant growth and development and for plant responses to abiotic and biotic stresses. In this study, a comprehensive identification of the PM H-ATPase gene family was conducted across four cotton species.
View Article and Find Full Text PDFThe P-type ATPase gene AHA5 is involved in proanthocyanidins accumulation in Medicago truncatula.
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Proanthocyanidins (PAs) are the second most abundant plant phenolic natural products. The proton membrane H-ATPase (AHA) is required for PA transportation in vacuoles, but it remains unclear which AHA gene(s) encode tonoplast proton pump in M. truncatula.
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College of Basic Medical Science, Jinzhou Medical University, Jinzhou, Liaoning, China.
Vacuolar-type H+-ATPase (V-ATPase) is a crucial proton pump that plays an essential role in maintaining intracellular pH homeostasis and a variety of physiological processes. This review provides an in-depth exploration of the structural components, functional mechanisms, and regulatory modes of V-ATPase in cancer cells. Comprising two main domains, V and V, V-ATPase drives the proton pump through ATP hydrolysis, sustaining the pH balance within the cell and organelles.
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