Samira Klössel, Ying Zhu, Lucia Amado, Daniel D Bisinski, Julia Ruta, Fan Liu, Ayelén González Montoro
The EMBO journal 2024 MayYeast vacuoles perform crucial cellular functions as acidic degradative organelles, storage compartments, and signaling hubs. These functions are mediated by important protein complexes, including the vacuolar-type H+-ATPase (V-ATPase), responsible for organelle acidification. To gain a more detailed understanding of vacuole function, we performed cross-linking mass spectrometry on isolated vacuoles, detecting many known as well as novel protein-protein interactions. Among these, we identified the uncharacterized TLDc-domain-containing protein Rtc5 as a novel interactor of the V-ATPase. We further analyzed the influence of Rtc5 and of Oxr1, the only other yeast TLDc-domain-containing protein, on V-ATPase function. We find that both Rtc5 and Oxr1 promote the disassembly of the vacuolar V-ATPase in vivo, counteracting the role of the RAVE complex, a V-ATPase assembly chaperone. Furthermore, Oxr1 is necessary for the retention of a Golgi-specific subunit of the V-ATPase in this compartment. Collectively, our results shed light on the in vivo roles of yeast TLDc-domain proteins as regulators of the V-ATPase, highlighting the multifaceted regulation of this crucial protein complex. © 2024. The Author(s).
Samira Klössel, Ying Zhu, Lucia Amado, Daniel D Bisinski, Julia Ruta, Fan Liu, Ayelén González Montoro. Yeast TLDc domain proteins regulate assembly state and subcellular localization of the V-ATPase. The EMBO journal. 2024 May;43(9):1870-1897
PMID: 38589611
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