3.A.2.2.6
H⁺-translocating V-type ATPase (Knight and Behm 2012). The c-subunit, ATP6V0C is upregulated by the drug against L. donovani, naloxonazine (De Muylder et al. 2016). ATP6V1B1 is present in elevated amounts in the ionocytes of several mammalian tissues (Pou Casellas et al. 2023).  The catalytic F₁ head rotates with the central γ-subunit for the first part of each ATP-generating power stroke. Joint rotation is enabled by subunit δ/OSCP acting as a flexible hinge between F₁ and the peripheral stalk. Subunit a conducts protons to and from the c-ring rotor through two conserved aqueous channels. The channels are separated by ∼6 Å in the hydrophobic core of F_o, resulting in a strong local field that generates torque to drive rotary catalysis in F₁. The structure of the chloroplast F₁F_o complex explains how ATPase activity is turned off at night by a redox switch. Structures of mitochondrial ATP synthase dimers indicate how they shape the inner membrane cristae (Kühlbrandt 2019). Prosapogenin A (PA) may act as a V-ATPase agonist, targeting lysosomal acidification, presenting a new potential therapeutic option for ATC treatment (Liu et al. 2024).  Golgi pH elevation due to loss of V-ATPase subunit V0a2 function correlates with tissue-specific glycosylation changes and globozoospermia (Kopp et al. 2024).  Variants of the ATP6V0A4 gene can give rise to neonatal onset distal renal tubular acidosis (Antoniadi et al. 2024).