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Role of Vacuolar Acidification in Protein Sorting and Zymogen Activation: a Genetic Analysis of the Yeast Vacuolar Proton-Translocating ATPase [PDF]
Molecular and Cellular Biology, 1990 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).
Carl T. Yamashiro +4 more
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Assembly of the yeast vacuolar proton-translocating ATPase.
Journal of bioenergetics and biomembranes, 1999 The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. Biochemical and genetic screens led to the identification of a large number of genes in yeast, designated VMA, encoding proteins required to assemble a functional V-ATPase.
Laurie A. Graham, Tom H. Stevens
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Journal of Investigative Dermatology, 1991 Langerhans cells (LC) are the principal antigen-presenting cells (APC) of squamous epithelia. We have previously shown that freshly isolated LC (fLC) are able to deliver endocytosed membrane MHC class II molecules into acidic environments, and that this capacity is lost when LC are placed in culture (cLC).
Giampiero Girolomoni +3 more
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Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase
Journal of Bioenergetics and Biomembranes, 1992 The yeast vacuole is acidified by a vacuolar proton-translocating ATPase (H(+)-ATPase) that closely resembles the vacuolar H(+)-ATPases of other fungi, animals, and plants. The yeast enzyme is purified as a complex of eight subunits, which include both integral and peripheral membrane proteins.
Patricia M. Kane, Tom H. Stevens
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Mouse Atp6f, the gene encoding the 23-kDa proteolipid of vacuolar proton translocating ATPase
Gene, 2001 The 23-kDa proteolipid subunit of mouse vacuolar-type proton-translocating ATPase (V-ATPase) was predicted to be a hydrophobic polypeptide of 205 amino acid residues with five putative transmembrane segments. It exhibits sequence similarity to Vma16p of Saccharomyces cerevisiae and vha-4 of Caenorhabdittis elegans (83 and 84%, respectively).
Ge‐Hong Sun‐Wada +4 more
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Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase
Biochemistry, 1996 In order to generate a set of tools for probing structure-function relationships in the catalytic subunit of the yeast vacuolar H(+)-ATPase, the gene encoding this subunit (VMA1) was randomly mutagenized. Mutant plasmids unable to complement the growth defects of yeast cells lacking an intact VMA1 gene were isolated and sequenced.
Jianzhong Liu, Patricia M. Kane
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2018 Karlett J. Parra, Summer R. Hayek
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Journal of Cell Science, 1996 ABSTRACT We have investigated the effects of Concanamycin A (CMA), a specific inhibitor of vacuolar type H+-ATPases, on acidification and function of the endo-lysosomal and contractile vacuole (CV) systems of D. discoideum. This drug inhibited acidification and increased the pH of endo-lysosomal vesicles both in vivo and in vitro in a ...
Lesly A. Temesvari +4 more
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Protein sorting in yeast: the role of the vacuolar protontranslocating ATPase
Journal of Cell Science, 1989ABSTRACT We are investigating the physiological roles of organelle acidification in yeast by two different approaches. First, we have identified two mutants which are defective in acidification of the yeast lysosome-like vacuole from among a collection of mutants which mis-sort soluble vacuolar proteins to the cell surface. These mutants
P M, Kane +3 more
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