Interaction of yeast V-ATPase with TLDc protein Rtc5p.

ABSTRACT: The eukaryotic vacuolar H⁺-ATPase (V-ATPase) is regulated by reversible disassembly into autoinhibited V₁-ATPase and V_o proton channel subcomplexes, a mode of regulation conserved from yeast to humans. While signals that govern V-ATPase assembly have been studied in the cellular context, the molecular mechanisms of the process at the level of the enzyme remain poorly understood. We recently discovered that Oxr1p, one of the two TLDc domain proteins in yeast, is essential for rapid V-ATPase disassembly in vivo. How the second TLDc protein, Rtc5p, functions in reversible disassembly, however, is less clear. Here we find that Rtc5p promotes assembly of functional holo V-ATPase from purified V₁ and V_o subcomplexes in vitro. C

SUBMITTER: Khan MM 

PROVIDER: S-EPMC12139955 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature