Results 11 to 20 of about 2,525 (167)

Vacuolar Acidification and Bafilomycin-Sensitive Proton Translocating ATPase in Human Epidermal Langerhans Cells

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).
GIROLOMONI, Giampiero, Stone DK, Bergstresser PR, Cruz P.D.   +3 more
openaire   +4 more sources

Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase) [PDF]

Journal of Biological Chemistry, 2012
Vacuolar proton-translocating ATPase (V-ATPase) is a central regulator of cellular pH homeostasis, and inactivation of all V-ATPase function has been shown to prevent infectivity in Candida albicans. V-ATPase subunit a of the Vo domain (Voa) is present as two fungal isoforms: Stv1p (Golgi) and Vph1p (vacuole).
Gregory C. Finnigan, Glen E. Cronan, Hae J. Park, Sankaranarayanan Srinivasan, Florante A. Quiocho, Tom H. Stevens   +5 more
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Conformation of a Peptide Encompassing the Proton Translocation Channel of Vacuolar H+-ATPase [PDF]

Biophysical Journal, 2007
The structural properties of a crucial transmembrane helix for proton translocation in vacuolar ATPase are studied using double site-directed spin-labeling combined with electron spin resonance (ESR) (or electron paramagnetic resonance) and circular dichroism spectroscopy in sodium dodecyl sulfate micelles.
Vos, W.L., Vermeer, L.S., Hemminga, M.A.
openaire   +3 more sources

V1-situated Stalk Subunits of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
The proton-translocating ATPase of the yeast vacuole is an enzyme complex consisting of a large peripheral membrane sector (V1) and an integral membrane sector (V0), each composed of multiple subunits. The V1 sector contains subunits that hydrolyze ATP, whereas the V0 sector contains subunits that translocate protons across the membrane.
J J, Tomashek, L A, Graham, M U, Hutchins, T H, Stevens, D J, Klionsky   +4 more
openaire   +2 more sources

Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy [PDF]

Frontiers in Pharmacology, 2014
Vacuolar proton-translocating ATPase (V-ATPase) is a membrane-bound, multi-subunit enzyme that uses the energy of ATP hydrolysis to pump protons across membranes. V-ATPase activity is critical for pH homeostasis and organelle acidification as well as for generation of the membrane potential that drives secondary transporters and cellular metabolism.
Summer R. Hayek, Samuel A. Lee, Samuel A. Lee, Karlett J. Parra   +3 more
openaire   +3 more sources

Identification and Reconstitution of an Isoform of the 116-kDa Subunit of the Vacuolar Proton Translocating ATPase [PDF]

Journal of Biological Chemistry, 1999
We have identified a cDNA encoding an isoform of the 116-kDa subunit of the bovine vacuolar proton translocating ATPase. The predicted protein sequence of the new isoform, designated a2, consists of 854 amino acids with a calculated molecular mass of 98,010 Da; it has approximately 50% identity to the original isoform (a1) we described (Peng, S.-B ...
S B, Peng, X, Li, B P, Crider, Z, Zhou, P, Andersen, S J, Tsai, X S, Xie, D K, Stone   +7 more
openaire   +2 more sources

Resolution of Subunit Interactions and Cytoplasmic Subcomplexes of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1996
The vacuolar proton-translocating ATPase is the principal energization mechanism that enables the yeast vacuole to perform most of its physiological functions. We have undertaken an examination of subunit-subunit interactions and assembly states of this enzyme.
J J, Tomashek, J L, Sonnenburg, J M, Artimovich, D J, Klionsky   +3 more
openaire   +2 more sources

Mutational Analysis of the Nucleotide Binding Sites of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1998
To further define the structure of the nucleotide binding sites on the vacuolar proton-translocating ATPase (V-ATPase), the role of aromatic residues at the catalytic sites was probed using site-directed mutagenesis of the VMA1 gene that encodes the A subunit in yeast.
K J, MacLeod, E, Vasilyeva, J D, Baleja, M, Forgac   +3 more
openaire   +2 more sources

Loss of Vacuolar Proton-translocating ATPase Activity in Yeast Results in Chronic Oxidative Stress [PDF]

Journal of Biological Chemistry, 2007
Yeast mutants lacking vacuolar proton-translocating ATPase (V-ATPase) subunits (vma mutants) were sensitive to several different oxidants in a recent genomic screen (Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 6564-6569). We confirmed that mutants lacking a V(1) subunit (vma2Delta),
Elena, Milgrom, Heba, Diab, Frank, Middleton, Patricia M, Kane   +3 more
openaire   +2 more sources

Regulation of vacuolar H+-ATPase activity by the Cdc42 effector Ste20 in Saccharomyces cerevisiae [PDF]

, 2012
In the budding yeast Saccharomyces cerevisiae, the Cdc42 effector Ste20 plays a crucial role in the regulation of filamentous growth, a response to nutrient limitation.
Höfken, T, Lin, M, Kane, PM, Li, SC
core   +1 more source