V-ATPase Disassembly at the Yeast Lysosome-Like Vacuole Is a Phenotypic Driver of Lysosome Dysfunction in Replicative Aging.

Declines in lysosomal acidification and function with aging are observed in organisms ranging from yeast to humans. V-ATPases play a central role in organelle acidification, and V-ATPase activity is regulated by reversible disassembly in many different settings. Using the yeast Saccharomyces cerevisiae as a replicative aging model, we demonstrate that V-ATPases disassemble into their V and V subcomplexes in aging cells, with release of V subunit C (Vma5) from the lysosome-like vacuole into the cytosol.

Newborn daughters get a fresh start through PI(3,5)P2-mediated vacuolar acidification.

Huda et al. (https://doi.org/10.

Structure of yeast RAVE bound to a partial V complex.

Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases, these multisubunit enzymes consist of a soluble catalytic V subcomplex and a membrane-embedded proton-translocating V subcomplex. The V and V subcomplexes can undergo reversible dissociation to regulate proton pumping, with reassociation of V and V requiring the protein complex known as RAVE (regulator of the ATPase of vacuoles and endosomes).

Unacceptable Behaviors Towards Health Professional Clinical Students: Protocol For a Mixed-Methods Study.

Background And Aims: Previous studies describe the occurrence of unacceptable behaviors reported by students pursuing health professional education in Aotearoa, New Zealand and across the globe. These include, but are not limited to, experiences of verbal abuse, sexual harassment, and discrimination based on race/ethnicity, religious beliefs, gender, and sexual orientation. University of Otago teaching staff across the various health professional programs often receive anecdotal reports of these phenomena from their clinical students.