The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.

Manolson, Morris F.; Proteau, D.; Preston, Robert A.; Stenbit, Antine E.; Roberts, B T; Hoyt, M. Andrew; Preuss, Daphne; Mulholland, Jon; Botstein, David; Jones, Elizabeth W.

doi:10.1016/s0021-9258(19)49711-1

Cited by 247 publications

(34 citation statements)

References 64 publications

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“…Owing to the large size of vacuoles, their number per cell was determined in fluorescence microscopy images of Vph1-GFP ( Manolson et al, 1992 ) cells by manually counting ≥200 cells per replicate and time point in Fiji ( Schindelin et al, 2012 ). Vacuolar area was quantified for ≥200 vacuoles per replicate and time point using the freehand area tool in Fiji on maximum projections of microscopy images of Vph1-GFP cells.…”

Section: Methodsmentioning

confidence: 99%

Large organellar changes occur during mild heat shock in yeast

Keuenhof

Berglund

Hill

et al. 2021

Journal of Cell Science

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When the temperature is increased, the heat shock response is activated to protect the cellular environment. The transcriptomics and proteomics of this process are intensively studied, while information about how the cell responds structurally to heat stress is mostly lacking. Here, Saccharomyces cerevisiae were subjected to a mild continuous heat shock (38°C) and intermittently cryo-immobilized for electron microscopy. Through measuring changes in all distinguishable organelle numbers, sizes, and morphologies in over 2100 electron micrographs a major restructuring of the cell's internal architecture during the progressive heat shock was revealed. The cell grew larger but most organelles within it expanded even more, shrinking the volume of the cytoplasm. Organelles responded to heat shock at different times, both in terms of size and number, and adaptations of certain organelles’ morphology (such as the vacuole), were observed. Multivesicular bodies grew to almost 170% in size, indicating a previously unknown involvement in the heat shock response. A previously undescribed electron translucent structure accumulated close to the plasma membrane. This all-encompassing approach provides a detailed chronological progression of organelle adaptation throughout the cellular heat-stress response.

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Section: Methodsmentioning

confidence: 99%

Large organellar changes occur during mild heat shock in yeast

Keuenhof

Berglund

Hill

et al. 2021

Journal of Cell Science

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“…LDs internalized into the vacuole only release their stored lipids when pH-sensitive vacuole lipases are active to digest the LDs. We tested whether the vacuole Lo domains play a role in facilitating this turnover by examining the vacuole distribution and activity of Vph1p, the Vo component of the vacuole proton pump (i.e., V-ATPase), which acidifies the vacuole by delivering protons into it (Manolson et al, 1992). Using Vac8-GFP to label Lo domains (Peng et al, 2006;, we found that in response to acute GR, Vph1p partitioned to the Ld phase surrounding Lo domains on the vacuole surface (Figure 6A), as previously reported Tsuji et al, 2017).…”

Section: Vacuole Phase Partitioning Leads To Increased Vacuole Aciditymentioning

confidence: 99%

Vacuole phase-partitioning boosts mitochondria activity and cell lifespan through an inter-organelle lipid pipeline

Seo

Sarkleti

Budin

et al. 2021

Preprint

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Functional linkage between mitochondria and lysosomes is crucial for survival under starvation and lifespan extension. Despite such co-dependency, the supportive pathways connecting mitochondria and lysosomes remain unclear. Here, we identify an inter-organelle lipid trafficking pathway linking yeast vacuole and mitochondria that results in increased mitochondria growth and respiratory activity under glucose starvation. The pathway depends on vacuolar phase-separated, lipid domains, which provide zones for: activation of the vacuolar proton pump; lipid droplet (LD) docking and internalization; and, lipid transfer from vacuole-to-ER-to-mitochondria. Partitioned vacuolar domains form through a specialized type of macro-autophagy, triggered only under acute glucose starvation, that delivers sterol-rich, endosomal-derived lipids to the vacuole. To balance this lipid influx, the vacuole reroutes lipids back to the ER to support both LD biogenesis and mitochondria growth and activity. Energy produced by enhanced mitochondrial activity then feeds back to support the inter-organelle lipid trafficking pathways to ensure survival under nutrient stress.

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“…In S. cerevisiae, Vph1p or Stv1p is included in the V-ATPase complex as the 'a' subunit, and the Stv1 protein (similar to Vph1p) is a paralog of Vph1p [28][29][30][31]. Vph1p is localized to the vacuoles, whereas Stv1p is present in the Golgi apparatus or other compartments, which are endosome compartments, and acts as a V-ATPase [29][30][31].…”

Section: Discussionmentioning

confidence: 99%

A capsule-associated gene of Cryptococcus neoformans, CAP64, is involved in pH homeostasis

et al. 2021

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The CAP64 gene is known to be involved in capsule formation in the basidiomycete yeast Cryptococcus neoformans. A null mutant of CAP64, Δcap64, lacks a capsule around the cell wall and its acidic organelles are not stained with quinacrine. In order to clarify whether the Cap64 protein indeed maintains vacuole or vesicle acidification, so that the vesicle containing the capsule polysaccharide or DBB substrate are transported to the cell membrane side, the relationship between CAP64 and intracellular transport genes and between CAP64 and enzyme-secretion activity were analysed. Laccase activity was higher in the Δcap64 strain than in the wild-type strain, and the transcriptional levels of SAV1 and VPH1 were also higher in the Δcap64 strain than in the wild-type strain. The intracellular localization of the Cap64 protein was analysed by overexpressing an mCherry-tagged Cap64 and observing its fluorescence. The Cap64 protein was accumulated within cells in a patch-like manner. The quinacrine-stained cells were observed to analyse the acidified cell compartments; quinacrine was found to be accumulated in a patch-like manner, with the patches overlapping the fluorescence of CAP64-mCherry fusion protein. Quinacrine was thus accumulated in a patch-like fashion in the cells, and the mCherry-tagged Cap64 protein position was consistent with the position of quinacrine accumulation in cells. These results suggest that CAP64 might be involved in intracellular acidification and vesicle secretion via exocytosis.

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The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.

Cited by 247 publications

References 64 publications

Large organellar changes occur during mild heat shock in yeast

Large organellar changes occur during mild heat shock in yeast

Vacuole phase-partitioning boosts mitochondria activity and cell lifespan through an inter-organelle lipid pipeline

A capsule-associated gene of Cryptococcus neoformans, CAP64, is involved in pH homeostasis

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