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Journal articles on the topic 'Vacuolar acidification'

Author: Grafiati

Published: 11 March 2023

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1

Yamashiro, C. T., P. M. Kane, D. F. Wolczyk, R. A. Preston, and T. H. Stevens. "Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase." Molecular and Cellular Biology 10, no. 7 (1990): 3737–49. http://dx.doi.org/10.1128/mcb.10.7.3737-3749.1990.

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Vacuolar acidification has been proposed to play a key role in a number of cellular processes, including protein sorting, zymogen activation, and maintenance of intracellular pH. We investigated the significance of vacuolar acidification by cloning and mutagenizing the gene for the yeast vacuolar proton-translocating ATPase 60-kilodalton subunit (VAT2). Cells carrying a vat2 null allele were viable; however, these cells were severely defective for growth in medium buffered at neutral pH. Vacuoles isolated from cells bearing the vat2 null allele were completely devoid of vacuolar ATPase activit

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2

Yamashiro, C. T., P. M. Kane, D. F. Wolczyk, R. A. Preston, and T. H. Stevens. "Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase." Molecular and Cellular Biology 10, no. 7 (1990): 3737–49. http://dx.doi.org/10.1128/mcb.10.7.3737.

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Vacuolar acidification has been proposed to play a key role in a number of cellular processes, including protein sorting, zymogen activation, and maintenance of intracellular pH. We investigated the significance of vacuolar acidification by cloning and mutagenizing the gene for the yeast vacuolar proton-translocating ATPase 60-kilodalton subunit (VAT2). Cells carrying a vat2 null allele were viable; however, these cells were severely defective for growth in medium buffered at neutral pH. Vacuoles isolated from cells bearing the vat2 null allele were completely devoid of vacuolar ATPase activit

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3

Morano, K. A., and D. J. Klionsky. "Differential effects of compartment deacidification on the targeting of membrane and soluble proteins to the vacuole in yeast." Journal of Cell Science 107, no. 10 (1994): 2813–24. http://dx.doi.org/10.1242/jcs.107.10.2813.

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Lysosomal/vacuolar protein targeting is dependent on compartment acidification. In yeast, sorting of soluble vacuolar proteins such as carboxypeptidase Y is sensitive to acute changes in vacuolar pH. In contrast, the vacuolar membrane protein alkaline phosphatase is missorted only under conditions of chronic deacidification. We have undertaken a temporal analysis to define further the relationship between compartment acidification and sorting of soluble and membrane vacuolar proteins. Depletion of either the Vma3p or Vma4p subunits of the yeast vacuolar ATPase over time resulted in loss of vac

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Chen, Shuliang, Maureen Tarsio, Patricia M. Kane, and Miriam L. Greenberg. "Cardiolipin Mediates Cross-Talk between Mitochondria and the Vacuole." Molecular Biology of the Cell 19, no. 12 (2008): 5047–58. http://dx.doi.org/10.1091/mbc.e08-05-0486.

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Cardiolipin (CL) is an anionic phospholipid with a dimeric structure predominantly localized in the mitochondrial inner membrane, where it is closely associated with mitochondrial function, biogenesis, and genome stability ( Daum, 1985 ; Janitor and Subik, 1993 ; Jiang et al., 2000 ; Schlame et al., 2000 ; Zhong et al., 2004 ). Previous studies have shown that yeast mutant cells lacking CL due to a disruption in CRD1, the structural gene encoding CL synthase, exhibit defective colony formation at elevated temperature even on glucose medium ( Jiang et al., 1999 ; Zhong et al., 2004 ), suggestin

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Raymond, C. K., I. Howald-Stevenson, C. A. Vater, and T. H. Stevens. "Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants." Molecular Biology of the Cell 3, no. 12 (1992): 1389–402. http://dx.doi.org/10.1091/mbc.3.12.1389.

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The collection of vacuolar protein sorting mutants (vps mutants) in Saccharomyces cerevisiae comprises of 41 complementation groups. The vacuoles in these mutant strains were examined using immunofluorescence microscopy. Most of the vps mutants were found to possess vacuolar morphologies that differed significantly from wild-type vacuoles. Furthermore, mutants representing independent vps complementation groups were found to share aberrant morphological features. Six distinct classes of vacuolar morphology were observed. Mutants from eight vps complementation groups were defective both for vac

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Raymond, C. K., P. J. O'Hara, G. Eichinger, J. H. Rothman, and T. H. Stevens. "Molecular analysis of the yeast VPS3 gene and the role of its product in vacuolar protein sorting and vacuolar segregation during the cell cycle." Journal of Cell Biology 111, no. 3 (1990): 877–92. http://dx.doi.org/10.1083/jcb.111.3.877.

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vps3 mutants of the yeast Saccharomyces cerevisiae are impaired in the sorting of newly synthesized soluble vacuolar proteins and in the acidification of the vacuole (Rothman, J. H., and T. H. Stevens. Cell. 47:1041-1051; Rothman, J. H., C. T. Yamashiro, C. K. Raymond, P. M. Kane, and T. H. Stevens. 1989. J. Cell Biol. 109:93-100). The VPS3 gene, which was cloned using a novel selection procedure, encodes a low abundance, hydrophilic protein of 117 kD that most likely resides in the cytoplasm. Yeast strains bearing a deletion of the VPS3 gene (vps3-delta 1) are viable, yet their growth rate is

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Rothman, J. H., C. T. Yamashiro, C. K. Raymond, P. M. Kane, and T. H. Stevens. "Acidification of the lysosome-like vacuole and the vacuolar H+-ATPase are deficient in two yeast mutants that fail to sort vacuolar proteins." Journal of Cell Biology 109, no. 1 (1989): 93–100. http://dx.doi.org/10.1083/jcb.109.1.93.

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Organelle acidification plays a demonstrable role in intracellular protein processing, transport, and sorting in animal cells. We investigated the relationship between acidification and protein sorting in yeast by treating yeast cells with ammonium chloride and found that this lysosomotropic agent caused the mislocalization of a substantial fraction of the newly synthesized vacuolar (lysosomal) enzyme proteinase A (PrA) to the cell surface. We have also determined that a subset of the vpl mutants, which are deficient in sorting of vacuolar proteins (Rothman, J. H., and T. H. Stevens. 1986. Cel

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8

Klionsky, D. J., H. Nelson, N. Nelson, and D. S. Yaver. "Mutations in the yeast vacuolar ATPase result in the mislocalization of vacuolar proteins." Journal of Experimental Biology 172, no. 1 (1992): 83–92. http://dx.doi.org/10.1242/jeb.172.1.83.

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The vacuolar ATPase of the yeast Saccharomyces cerevisiae acidifies the vacuolar lumen and generates an electrochemical gradient across the vacuole membrane. We have investigated the role of compartment acidification of the vacuolar system in the sorting of vacuolar proteins. Strains with chromosomal disruptions of genes (delta vat) encoding the A (69 x 10(3) M(r)), B (57 x 10(3) M(r)) or c (16 x 10(3) M(r)) subunits of the vacuolar ATPase accumulate and secrete precursor forms of the soluble vacuolar hydrolases carboxypeptidase Y and proteinase A. A kinetic analysis suggests that these precur

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Banta, L. M., J. S. Robinson, D. J. Klionsky, and S. D. Emr. "Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting." Journal of Cell Biology 107, no. 4 (1988): 1369–83. http://dx.doi.org/10.1083/jcb.107.4.1369.

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Yeast vacuole protein targeting (vpt) mutants exhibit defects in the sorting and processing of multiple vacuolar hydrolases. To evaluate the impact these vpt mutations have on the biogenesis and functioning of the lysosome-like vacuole, we have used light and electron microscopic techniques to analyze the vacuolar morphology in the mutants. These observations have permitted us to assign the vpt mutants to three distinct classes. The class A vpt mutants (26 complementation groups) contain 1-3 large vacuoles that are morphologically indistinguishable from those in the parental strain, suggesting

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Steele-Mortimer, Olivia, Maryse St-Louis, Martin Olivier, and B. Brett Finlay. "Vacuole Acidification Is Not Required for Survival ofSalmonella enterica Serovar Typhimurium within Cultured Macrophages and Epithelial Cells." Infection and Immunity 68, no. 9 (2000): 5401–4. http://dx.doi.org/10.1128/iai.68.9.5401-5404.2000.

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ABSTRACT Phagosome acidification is an important component of the microbicidal response by infected eukaryotic cells. Thus, intracellular pathogens that reside within phagosomes must either block phagosome acidification or be able to survive at low pH. In this work, we studied the effect of phagosomal acidification on the survival of intracellular Salmonella enterica serovar Typhimurium in different cell types. Bafilomycin A1, a specific inhibitor of the vacuolar proton-ATPases, was used to block acidification of salmonella-containing vacuoles. We found that in several epithelial cell lines, t

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Voynova, Natalia S., Carole Roubaty, Hector M. Vazquez, Shamroop K. Mallela, Christer S. Ejsing, and Andreas Conzelmann. "Saccharomyces cerevisiae Is Dependent on Vesicular Traffic between the Golgi Apparatus and the Vacuole When Inositolphosphorylceramide Synthase Aur1 Is Inactivated." Eukaryotic Cell 14, no. 12 (2015): 1203–16. http://dx.doi.org/10.1128/ec.00117-15.

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ABSTRACTInositolphosphorylceramide (IPC) and its mannosylated derivatives are the only complex sphingolipids of yeast. Their synthesis can be reduced by aureobasidin A (AbA), which specifically inhibits the IPC synthase Aur1. AbA reportedly, by diminishing IPC levels, causes endoplasmic reticulum (ER) stress, an increase in cytosolic calcium, reactive oxygen production, and mitochondrial damage leading to apoptosis. We found that when Aur1 is gradually depleted by transcriptional downregulation, the accumulation of ceramides becomes a major hindrance to cell survival. Overexpression of the alk

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Forgac, M. "Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases." Journal of Experimental Biology 203, no. 1 (2000): 71–80. http://dx.doi.org/10.1242/jeb.203.1.71.

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The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps that carry out acidification of intracellular compartments in eukaryotic cells. This review is focused on our work on the V-ATPases of clathrin-coated vesicles and yeast vacuoles. The coated-vesicle V-ATPase undergoes trafficking to endosomes and synaptic vesicles, where it functions in receptor recycling and neurotransmitter uptake, respectively. The yeast V-ATPase functions to acidify the central vacuole and is necessary both for protein degradation and for coupled transport processes across the vacuolar memb

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13

Myers, M., and M. Forgac. "Mechanism and Function of Vacuolar Acidification." Physiology 8, no. 1 (1993): 24–29. http://dx.doi.org/10.1152/physiologyonline.1993.8.1.24.

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Vacuolar acidification plays an important role in such processes as receptor-mediated endocytosis, intracellular membrane traffic, and protein degradation. Vacuolar H+-adenosinetriphosphatases (ATPases) are responsible for this acidification.

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Bonangelino, C. J., N. L. Catlett, and L. S. Weisman. "Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology." Molecular and Cellular Biology 17, no. 12 (1997): 6847–58. http://dx.doi.org/10.1128/mcb.17.12.6847.

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During cell division, the vacuole of Saccharomyces cerevisiae partitions between mother and daughter cells. A portion of the parental vacuole membrane moves into the bud, and ultimately membrane scission divides the vacuole into two separate structures. Here we characterize two yeast mutations causing defects in vacuole membrane scission, vac7-1 and vac14-1. A third mutant, afab1-2 strain, isolated in a nonrelated screen (A. Yamamoto et al., Mol. Biol. Cell 6:525-539, 1995) shares the vacuolar phenotypes of the vac7-1 and vac14-1 strains. Unlike the wild type, mutant vacuoles are not multilobe

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Zhang, Chi, Adam Balutowski, Yilin Feng, Jorge D. Calderin, and Rutilio A. Fratti. "High throughput analysis of vacuolar acidification." Analytical Biochemistry 658 (December 2022): 114927. http://dx.doi.org/10.1016/j.ab.2022.114927.

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16

Ruckenstuhl, Christoph, Christine Netzberger, Iryna Entfellner, et al. "Autophagy extends lifespan via vacuolar acidification." Microbial Cell 1, no. 5 (2014): 160–62. http://dx.doi.org/10.15698/mic2014.05.147.

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17

Suriapranata, I., U. D. Epple, D. Bernreuther, M. Bredschneider, K. Sovarasteanu, and M. Thumm. "The breakdown of autophagic vesicles inside the vacuole depends on Aut4p." Journal of Cell Science 113, no. 22 (2000): 4025–33. http://dx.doi.org/10.1242/jcs.113.22.4025.

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Autophagy is a degradative transport pathway that delivers cytosolic proteins to the lysosome (vacuole). Cytosolic proteins appear inside the vacuole enclosed in autophagic vesicles. These autophagic vesicles are broken down in the vacuole together with their cytosolic content. The breakdown of vesicular transport intermediates is a unique feature of autophagy. We here identify Aut4p, a component essential for the disintegration of autophagic vesicles, inside the vacuole of S. cerevisiae cells. Aut4p is a putative integral membrane protein with limited homologies to permeases. Chromosomal dele

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18

Kane, P. M. "Biogenesis of the yeast vacuolar H(+)-ATPase." Journal of Experimental Biology 172, no. 1 (1992): 93–103. http://dx.doi.org/10.1242/jeb.172.1.93.

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Achieving an understanding of the biosynthesis, assembly and intracellular targeting of the vacuolar H(+)-ATPase is critical for understanding the distribution of acidic compartments and the regulation of organelle acidification. The assembly of the yeast vacuolar H(+)-ATPase requires the attachment of several cytoplasmically oriented, peripheral subunits (the V1 sector) to a complex of integral membrane subunits (the Vo sector) and thus is not easily described by the established mechanisms for transport of soluble or vacuolar membrane proteins to the vacuole. In order to examine the assembly

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Charoenbhakdi, Sirikarn, Thanittra Dokpikul, Thanawat Burphan, Todsapol Techo, and Choowong Auesukaree. "Vacuolar H+-ATPase Protects Saccharomyces cerevisiae Cells against Ethanol-Induced Oxidative and Cell Wall Stresses." Applied and Environmental Microbiology 82, no. 10 (2016): 3121–30. http://dx.doi.org/10.1128/aem.00376-16.

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ABSTRACTDuring fermentation, increased ethanol concentration is a major stress for yeast cells. Vacuolar H+-ATPase (V-ATPase), which plays an important role in the maintenance of intracellular pH homeostasis through vacuolar acidification, has been shown to be required for tolerance to straight-chain alcohols, including ethanol. Since ethanol is known to increase membrane permeability to protons, which then promotes intracellular acidification, it is possible that the V-ATPase is required for recovery from alcohol-induced intracellular acidification. In this study, we show that the effects of

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Smardon, Anne M., Heba I. Diab, Maureen Tarsio, et al. "The RAVE complex is an isoform-specific V-ATPase assembly factor in yeast." Molecular Biology of the Cell 25, no. 3 (2014): 356–67. http://dx.doi.org/10.1091/mbc.e13-05-0231.

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The regulator of ATPase of vacuoles and endosomes (RAVE) complex is implicated in vacuolar H+-translocating ATPase (V-ATPase) assembly and activity. In yeast, rav1∆ mutants exhibit a Vma− growth phenotype characteristic of loss of V-ATPase activity only at high temperature. Synthetic genetic analysis identified mutations that exhibit a full, temperature-independent Vma− growth defect when combined with the rav1∆ mutation. These include class E vps mutations, which compromise endosomal sorting. The synthetic Vma− growth defect could not be attributed to loss of vacuolar acidification in the dou

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OHKUMA, Shoji, Tomohiko SATO, Masayuki OKAMOTO, et al. "Prodigiosins uncouple lysosomal vacuolar-type ATPase through promotion of H+/Cl− symport." Biochemical Journal 334, no. 3 (1998): 731–41. http://dx.doi.org/10.1042/bj3340731.

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We reported previously [Kataoka, Muroi, Ohkuma, Waritani, Magae, Takatsuki, Kondo, Yamasaki and Nagai (1995) FEBS Lett. 359, 53–59] that prodigiosin 25-C (one of the red pigments of the prodigiosin group produced by micro-organisms like Streptomycesand Serratia) uncoupled vacuolar H+-ATPase, inhibited vacuolar acidification and affected glycoprotein processing. In the present study we show that prodigiosin, metacycloprodigiosin and prodigiosin 25-C, all raise intralysosomal pH through inhibition of lysosomal acidification driven by vacuolar-type (V-)ATPase without inhibiting ATP hydrolysis in

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Pérez-Castiñeira, José R., Agustín Hernández, Rocío Drake, and Aurelio Serrano. "A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast." Biochemical Journal 437, no. 2 (2011): 269–78. http://dx.doi.org/10.1042/bj20110447.

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V-ATPases (vacuolar H+-ATPases) are a specific class of multi-subunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. Another simpler proton pump that co-localizes with the V-ATPase occurs in plants and many protists: the single-subunit H+-PPase [H+-translocating PPase (inorganic pyrophosphatase)]. Little is known about the relative contribution of these two proteins to the acidification of intracellular compartments. In the present study, we show that the expression of a chimaeric derivative of the Arabidopsis thaliana H+-PPase AVP1, wh

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Kwon, Yun, Jinbo Shen, Myoung Hui Lee, Kyoung Rok Geem, Liwen Jiang, and Inhwan Hwang. "AtCAP2 is crucial for lytic vacuole biogenesis during germination by positively regulating vacuolar protein trafficking." Proceedings of the National Academy of Sciences 115, no. 7 (2018): E1675—E1683. http://dx.doi.org/10.1073/pnas.1717204115.

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Protein trafficking is a fundamental mechanism of subcellular organization and contributes to organellar biogenesis. AtCAP2 is an Arabidopsis homolog of the Mesembryanthemum crystallinum calcium-dependent protein kinase 1 adaptor protein 2 (McCAP2), a member of the syntaxin superfamily. Here, we show that AtCAP2 plays an important role in the conversion to the lytic vacuole (LV) during early plant development. The AtCAP2 loss-of-function mutant atcap2-1 displayed delays in protein storage vacuole (PSV) protein degradation, PSV fusion, LV acidification, and biosynthesis of several vacuolar prot

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24

Patenaude, Cassandra, Yongqiang Zhang, Brendan Cormack, Julia Köhler, and Rajini Rao. "Essential Role for Vacuolar Acidification inCandida albicansVirulence." Journal of Biological Chemistry 288, no. 36 (2013): 26256–64. http://dx.doi.org/10.1074/jbc.m113.494815.

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25

Martin-Orozco, Natalia, Nicolas Touret, Michael L. Zaharik, et al. "Visualization of Vacuolar Acidification-induced Transcription of Genes of Pathogens inside Macrophages." Molecular Biology of the Cell 17, no. 1 (2006): 498–510. http://dx.doi.org/10.1091/mbc.e04-12-1096.

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The objective of these studies was to analyze the role of the ionic environment of phagosomal vacuoles in the control of pathogens by macrophages. Digital imaging and flow cytometry were used to follow the induction of the phoP promoter of Salmonella enterica Typhimurium within live macrophages. Manipulating the Mg2+concentration within the Salmonella-containing vacuole (SCV) was without effect on the early induction of PhoPQ. Moreover, direct measurement of [Mg2+] within the SCV using nanosensor particles showed that, during this initial period of phoP activation, the concentration of the div

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Boutouja, Stiehm, Reidick, et al. "Vac8 Controls Vacuolar Membrane Dynamics during Different Autophagy Pathways in Saccharomyces cerevisiae." Cells 8, no. 7 (2019): 661. http://dx.doi.org/10.3390/cells8070661.

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The yeast vacuole is a vital organelle, which is required for the degradation of aberrant intracellular or extracellular substrates and the recycling of the resulting nutrients as newly available building blocks for the cellular metabolism. Like the plant vacuole or the mammalian lysosome, the yeast vacuole is the destination of biosynthetic trafficking pathways that transport the vacuolar enzymes required for its functions. Moreover, substrates destined for degradation, like extracellular endocytosed cargoes that are transported by endosomes/multivesicular bodies as well as intracellular subs

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Wang, Jia-Gang, Chong Feng, Hai-Hong Liu, Qiang-Nan Feng, Sha Li, and Yan Zhang. "AP1G mediates vacuolar acidification during synergid-controlled pollen tube reception." Proceedings of the National Academy of Sciences 114, no. 24 (2017): E4877—E4883. http://dx.doi.org/10.1073/pnas.1617967114.

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Double fertilization in angiosperms requires the delivery of immotile sperm through pollen tubes, which enter embryo sacs to initiate synergid degeneration and to discharge. This fascinating process, called pollen tube reception, involves extensive communications between pollen tubes and synergids, within which few intracellular regulators involved have been revealed. Here, we report that vacuolar acidification in synergids mediated by AP1G and V-ATPases might be critical for pollen tube reception. Functional loss of AP1G or VHA-A, encoding the γ subunit of adaptor protein 1 or the shared comp

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Manolson, M. F., D. Proteau, and E. W. Jones. "Evidence for a conserved 95-120 kDa subunit associated with and essential for activity of V-ATPases." Journal of Experimental Biology 172, no. 1 (1992): 105–12. http://dx.doi.org/10.1242/jeb.172.1.105.

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Vacuoles purified from Saccharomyces cerevisiae bearing the vph1-1 mutation had no detectable bafilomycin-sensitive ATPase activity or ATP-dependent proton pumping. Furthermore, the vacuolar H(+)-ATPase (V-ATPase) nucleotide binding subunits were no longer associated with vacuolar membranes yet were present at wild-type levels in yeast whole-cell extracts. The VPH1 gene was cloned by screening a lambda gt11 expression library with antibodies directed against a 95 kDa vacuolar integral membrane protein and independently cloned by complementation of the vph1-1 mutation. Deletion disruption of th

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Swanson, Sarah J., and Russell L. Jones. "Gibberellic Acid Induces Vacuolar Acidification in Barley Aleurone." Plant Cell 8, no. 12 (1996): 2211. http://dx.doi.org/10.2307/3870462.

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Feng, Y., and M. Forgac. "A novel mechanism for regulation of vacuolar acidification." Journal of Biological Chemistry 267, no. 28 (1992): 19769–72. http://dx.doi.org/10.1016/s0021-9258(19)88619-2.

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Bray, Patrick G., Robert E. Howells, and Stephen A. Ward. "Vacuolar acidification and chloroquine sensitivity in plasmodium falciparum." Biochemical Pharmacology 43, no. 6 (1992): 1219–27. http://dx.doi.org/10.1016/0006-2952(92)90495-5.

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Huynh, My-Hang, and Vern B. Carruthers. "Toxoplasma gondii excretion of glycolytic products is associated with acidification of the parasitophorous vacuole during parasite egress." PLOS Pathogens 18, no. 5 (2022): e1010139. http://dx.doi.org/10.1371/journal.ppat.1010139.

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The Toxoplasma gondii lytic cycle is a repetition of host cell invasion, replication, egress, and re-invasion into the next host cell. While the molecular players involved in egress have been studied in greater detail in recent years, the signals and pathways for triggering egress from the host cell have not been fully elucidated. A perforin-like protein, PLP1, has been shown to be necessary for permeabilizing the parasitophorous vacuole (PV) membrane or exit from the host cell. In vitro studies indicated that PLP1 is most active in acidic conditions, and indirect evidence using superecliptic

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Kleinman, J. G. "Proton ATPases and urinary acidification." Journal of the American Society of Nephrology 5, no. 5 (1994): S6. http://dx.doi.org/10.1681/asn.v55s6.

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Acidification of the urine is mediated by vectorial H+ transport from cells at a number of sites in the kidney. A proton ATPase has been described that appears to mediate a significant proportion of this H+ transport. In particular, in proximal tubule and collecting duct, there is evidence both for the presence of transporter protein and for H+ transport with features that have been identified with it. This review highlights some of the unresolved questions regarding this transporter, specifically, its distribution and relationship to the vacuolar pump present in endocytotic vesicles, how phys

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Oluwatosin, Yemisi E., and Patricia M. Kane. "Mutations in the Yeast KEX2 Gene Cause a Vma−-Like Phenotype: a Possible Role for the Kex2 Endoprotease in Vacuolar Acidification." Molecular and Cellular Biology 18, no. 3 (1998): 1534–43. http://dx.doi.org/10.1128/mcb.18.3.1534.

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ABSTRACT Mutants of Saccharomyces cerevisiae that lack vacuolar proton-translocating ATPase (V-ATPase) activity show a well-defined set of Vma− (stands for vacuolar membrane ATPase activity) phenotypes that include pH-conditional growth, increased calcium sensitivity, and the inability to grow on nonfermentable carbon sources. By screening based on these phenotypes and the inability ofvma mutants to accumulate the lysosomotropic dye quinacrine in their vacuoles, five new vma complementation groups (vma41 to vma45) were identified. TheVMA45 gene was cloned by complementation of the pH-condition

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Wada, Yoh, Yoshinori Ohsumi, and Yasuhiro Anraku. "Chloride transport of yeast vacuolar membrane vesicles: a study of in vitro vacuolar acidification." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1101, no. 3 (1992): 296–302. http://dx.doi.org/10.1016/0005-2728(92)90085-g.

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RODRIGUES, Claudia O., David A. SCOTT, and Roberto DOCAMPO. "Presence of a vacuolar H+-pyrophosphatase in promastigotes of Leishmania donovani and its localization to a different compartment from the vacuolar H+-ATPase." Biochemical Journal 340, no. 3 (1999): 759–66. http://dx.doi.org/10.1042/bj3400759.

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Inorganic pyrophosphate promoted the acidification of an intracellular compartment in permeabilized promastigotes of Leishmania donovani, as measured by Acridine Orange uptake. The proton gradient generated by pyrophosphate was collapsed by addition of nigericin or NH4Cl. Pyrophosphate-driven proton translocation was stimulated by potassium ions, and inhibited by NaF, the pyrophosphate analogues imidodiphosphate and aminomethylenediphosphonate (AMDP), dicyclohexylcarbodiimide, and the thiol reagents p-hydroxymercuribenzoate and N-ethylmaleimide, all at concentrations similar to those that inhi

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Poltermann, Sophia, Monika Nguyen, Juliane Günther, et al. "The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence." Microbiology 151, no. 5 (2005): 1645–55. http://dx.doi.org/10.1099/mic.0.27505-0.

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The vacuolar H+-ATPase (V-ATPase) component Vma7p of the human-pathogenic yeast Candida albicans regulates hyphal growth induced by serum and Spider medium and is essential for virulence. In order to characterize the functions of the putative V-ATPase subunit Vma7p of C. albicans, null mutants were generated. The resulting mutants showed reduced vacuole acidification, which correlated with defective growth at alkaline pH. In addition, defects in degradation of intravacuolar putative endosomal structures were observed. vma7 null mutants were sensitive towards the presence of metal ions. It is c

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MAQUOI, Erik, Karine PEYROLLIER, Agnès NOËL, Jean-Michel FOIDART, and Francis FRANKENNE. "Regulation of membrane-type 1 matrix metalloproteinase activity by vacuolar H+-ATPases." Biochemical Journal 373, no. 1 (2003): 19–24. http://dx.doi.org/10.1042/bj20030170.

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Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a key enzyme in normal development and malignant processes. The regulation of MT1-MMP activity on the cell surface is a complex process involving autocatalytic processing, tissue inhibitor of MMPs (TIMP) binding and constitutive internalization. However, the fate of internalized MT1-MMP is not known. Acidification of intracellular vacuolar compartments is essential for membrane trafficking, protein sorting and degradation. This acidification is controlled by vacuolar H+-ATPases, which can be selectively inhibited by bafilomycin-A1. Here, we

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Singer-Krüger, B., H. Stenmark, A. Düsterhöft, et al. "Role of three rab5-like GTPases, Ypt51p, Ypt52p, and Ypt53p, in the endocytic and vacuolar protein sorting pathways of yeast." Journal of Cell Biology 125, no. 2 (1994): 283–98. http://dx.doi.org/10.1083/jcb.125.2.283.

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The small GTPase rab5 has been shown to represent a key regulator in the endocytic pathway of mammalian cells. Using a PCR approach to identify rab5 homologs in Saccharomyces cerevisiae, two genes encoding proteins with 54 and 52% identity to rab5, YPT51 and YPT53 have been identified. Sequencing of the yeast chromosome XI has revealed a third rab5-like gene, YPT52, whose protein product exhibits a similar identity to rab5 and the other two YPT gene products. In addition to the high degree of identity/homology shared between rab5 and Ypt51p, Ypt52p, and Ypt53p, evidence for functional homology

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Brune, Andreas, Mathias Müller, Lincoln Taiz, Pedro Gonzalez, and Ed Etxeberria. "Vacuolar Acidification in Citrus Fruit: Comparison between Acid Lime (Citrus aurantifolia) and Sweet Lime (Citrus limmetioides) Juice Cells." Journal of the American Society for Horticultural Science 127, no. 2 (2002): 171–77. http://dx.doi.org/10.21273/jashs.127.2.171.

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Vacuolar acidification was investigated in `Palestine' sweet (Citrus limmetioides Tanaka) and `Persian' acid lime [(Citrus aurantifolia (Christm.) Swingle] (vacuolar pHs of 5.0 and 2.1, respectively) using tonoplast vesicles isolated from juice cells. The ATPase activity of tonoplast-enriched vesicles from sweet limes was strongly inhibited by bafilomycin A1 and NO3-, but was unaffected by vanadate. In contrast, the ATPase activity in acid lime membranes was only slightly inhibited by bafilomycin A1 and NO3- and was strongly inhibited by high concentrations of vanadate. The vacuolar origin of

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Johnson, L. S., K. W. Dunn, B. Pytowski, and T. E. McGraw. "Endosome acidification and receptor trafficking: bafilomycin A1 slows receptor externalization by a mechanism involving the receptor's internalization motif." Molecular Biology of the Cell 4, no. 12 (1993): 1251–66. http://dx.doi.org/10.1091/mbc.4.12.1251.

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To examine the relationship between endosome acidification and receptor trafficking, transferrin receptor trafficking was characterized in Chinese hamster ovary cells in which endosome acidification was blocked by treatment with the specific inhibitor of the vacuolar H(+)-ATPase, bafilomycin A1. Elevating endosome pH slowed the receptor externalization rate to approximately one-half of control but did not affect receptor internalization kinetics. The slowed receptor externalization required the receptor's cytoplasmic domain and was largely eliminated by substitutions replacing either of two ar

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Scholz-Starke, Joachim. "How may PI(3,5)P2 impact on vacuolar acidification?" Channels 11, no. 6 (2017): 497–98. http://dx.doi.org/10.1080/19336950.2017.1354584.

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Jung, Joo-Yong, and Cory M. Robinson. "Interleukin-27 inhibits phagosomal acidification by blocking vacuolar ATPases." Cytokine 62, no. 2 (2013): 202–5. http://dx.doi.org/10.1016/j.cyto.2013.03.010.

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Futai, M., T. Oka, G. Sun-Wada, Y. Moriyama, H. Kanazawa, and Y. Wada. "Luminal acidification of diverse organelles by V-ATPase in animal cells." Journal of Experimental Biology 203, no. 1 (2000): 107–16. http://dx.doi.org/10.1242/jeb.203.1.107.

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Eukaryotic cells contain organelles bounded by a single membrane in the cytoplasm. These organelles have differentiated to carry out various functions in the pathways of endocytosis and exocytosis. Their lumina are acidic, with pH ranging from 4.5 to 6.5. This article describes recent studies on these animal cell organelles focusing on (1) the primary proton pump (vacuolar-type H(+)-ATPase) and (2) the functions of the organelle luminal acidity. We also discuss similarities and differences between vacuolar-type H(+)-ATPase and F-type ATPase. Our own studies and interests are emphasized.

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Munn, A. L., and H. Riezman. "Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes." Journal of Cell Biology 127, no. 2 (1994): 373–86. http://dx.doi.org/10.1083/jcb.127.2.373.

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Yeast mutants that are defective in acidification of the lysosome-like vacuole are able to grow at pH 5.5, but not at pH 7. Here, we present evidence that endocytosis is required for this low pH-dependent growth and use this observation to develop a screen for mutants defective in endocytosis. By isolating mutants that cannot grow when they lack the 60-kD vacuolar ATPase subunit (encoded by the VAT2 gene), we isolated a number of vat2-synthetic lethal (Vsl-) mutant strains. Seven of the Vsl- mutants are defective in endocytosis. Four of these mutant strains (end8-1, end9-1, end10-1, and end11-

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Kataoka, Takao, Makoto Muroi, Shoji Ohkuma, et al. "Prodigiosin 25-C uncouples vacuolar type H+ -ATPase, inhibits vacuolar acidification and affects glycoprotein processing." FEBS Letters 359, no. 1 (1995): 53–59. http://dx.doi.org/10.1016/0014-5793(94)01446-8.

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Perzov, Natalie, Vered Padler-Karavani, Hannah Nelson, and Nathan Nelson. "Characterization of yeast V-ATPase mutants lacking Vph1p or Stv1p and the effect on endocytosis." Journal of Experimental Biology 205, no. 9 (2002): 1209–19. http://dx.doi.org/10.1242/jeb.205.9.1209.

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SUMMARYSubunit a of V-ATPase in the yeast Saccharomyces cerevisiae, in contrast to its other subunits, is encoded by two genes VPH1 and STV1. While disruption of any other gene encoding the V-ATPase subunits results in growth arrest at pH 7.5, null mutants of Vph1p or Stv1p can grow at this pH. We used a polyclonal antibody to yeast Stv1p and a commercially available monoclonal antibody to Vph1p for analysis of yeast membranes by sucrose gradient fractionation, and two different vital dyes to characterize the phenotype of vph1 ▵ and stv1 ▵mutants as compared to the double mutant and the wild-t

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Huang, Chunjuan, and Amy Chang. "pH-dependent Cargo Sorting from the Golgi." Journal of Biological Chemistry 286, no. 12 (2011): 10058–65. http://dx.doi.org/10.1074/jbc.m110.197889.

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The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Deficiency of V-ATPase activity caused by subunit deletion or glucose deprivation results in missorting of newly synthesized plasma membrane proteins Pma1 and Can1 directly from the Golgi to the vacuole. Vacuolar mislocalization of Pma1 is dependent on Gga adaptors although no Pma1 ubiquitination was de

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de Castro, Patrícia Alves, Marcela Savoldi, Diego Bonatto, et al. "Molecular Characterization of Propolis-Induced Cell Death in Saccharomyces cerevisiae." Eukaryotic Cell 10, no. 3 (2010): 398–411. http://dx.doi.org/10.1128/ec.00256-10.

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ABSTRACTPropolis, a natural product of plant resins, is used by the bees to seal holes in their honeycombs and protect the hive entrance. However, propolis has also been used in folk medicine for centuries. Here, we apply the power ofSaccharomyces cerevisiaeas a model organism for studies of genetics, cell biology, and genomics to determine how propolis affects fungi at the cellular level. Propolis is able to induce an apoptosis cell death response. However, increased exposure to propolis provides a corresponding increase in the necrosis response. We showed that cytochromecbut not endonuclease

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Lang, Thomas, Steffen Reiche, Michael Straub, Monika Bredschneider, and Michael Thumm. "Autophagy and the cvt Pathway Both Depend onAUT9." Journal of Bacteriology 182, no. 8 (2000): 2125–33. http://dx.doi.org/10.1128/jb.182.8.2125-2133.2000.

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ABSTRACT In growing cells of the yeast Saccharomyces cerevisiae, proaminopeptidase I reaches the vacuole via the selective cytoplasm-to-vacuole targeting (cvt) pathway. During nutrient limitation, autophagy is also responsible for the transport of proaminopeptidase I. These two nonclassical protein transport pathways to the vacuole are distinct in their characteristics but in large part use identical components. We expanded our initial screen foraut − mutants and isolated aut9-1cells, which show a defect in both pathways, the vacuolar targeting of proaminopeptidase I and autophagy. By compleme

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