Results 11 to 20 of about 2,277 (122)

The Lack of a COPII Cargo Receptor Erv14 Impacts Physiological Functions of the Vacuole in Saccharomyces cerevisiae. [PDF]

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Loss of the cargo receptor Erv14 in Saccharomyces cerevisiae results in sensitivity to calcium, zinc, neutral extracellular pH, and elevated temperature. Furthermore, cells deleted in the ERV14 exhibits vacuolar fragmentation, enlarged lipid droplets, and metabolic alterations. Ruiz Salas, J. L. (2026) https://BioRender.com/b65g523. ABSTRACT Erv14 is a
Rosas-Santiago P, Salas JLR, Cordoba E, Portillo FV, Salas-Navarrete PC, Cabrera JAP, Martínez A, Ramírez NIR, Hernández DC, Saralegui-Amaro A, Calahorra M, Sychrová H, Zimmermannová O.   +12 more
europepmc   +2 more sources

The role of the host—Neutrophil biology

Periodontology 2000, EarlyView., 2023
Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple, Josefine Hirschfeld, Alpdogan Kantarci, Asaf Wilensky, Lior Shapira   +4 more
wiley   +1 more source

The Presynaptic v-ATPase Reversibly Disassembles and Thereby Modulates Exocytosis but Is Not Part of the Fusion Machinery

Cell Reports, 2017
Vacuolar H+-ATPase (v-ATPase) is a multi-subunit complex comprising two domains: the cytosolic V1 domain catalyzing ATP hydrolysis and the membranous V0 sector translocating protons across membranes.
Anna Bodzęta, Martin Kahms, Jürgen Klingauf   +2 more
doaj   +1 more source

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

Reconstitution in Vitro of the V1 Complex from the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
Oligomeric assembly is a fundamental aspect of many complex enzymes. Using our native gel technique for examining subcomplexes of the V-ATPase V1 sector, we have developed an in vitro reconstitution assay for assembly of this complex. Assembly of complex II, the soluble V1 complex observed in native gels, is dependent upon the presence of divalent ...
John J. Tomashek, Brian S. Garrison, Daniel J. Klionsky   +2 more
openaire   +2 more sources

Vacuolar proton-translocating ATPase is required for antifungal resistance and virulence of Candida glabrata

PLOS ONE, 2019
Vacuolar proton-translocating ATPase (V-ATPase) is located in fungal vacuolar membranes. It is involved in multiple cellular processes, including the maintenance of intracellular ion homeostasis by maintaining acidic pH within the cell. The importance of V-ATPase in virulence has been demonstrated in several pathogenic fungi, including Candida albicans.
Asuka Minematsu, Taiga Miyazaki, Shintaro Shimamura, Hiroshi Nishikawa, Hironobu Nakayama, Takahiro Takazono, Tomomi Saijo, Kazuko Yamamoto, Yoshifumi Imamura, Katsunori Yanagihara, Shigeru Kohno, Hiroshi Mukae, Koichi Izumikawa   +12 more
openaire   +5 more sources

Transmembrane Topography of the 100-kDa a Subunit (Vph1p) of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1999
The membrane topography of the yeast vacuolar proton-translocating ATPase a subunit (Vph1p) has been investigated using cysteine-scanning mutagenesis. A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity.
X H, Leng, T, Nishi, M, Forgac
openaire   +2 more sources

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).
C T, Yamashiro, P M, Kane, D F, Wolczyk, R A, Preston, T H, Stevens   +4 more
openaire   +2 more sources

The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections [PDF]

British Journal of Pharmacology, 2011
Cellular vacuolar ATPases (v-ATPase) play an important role in endosomal acidification, a critical step in influenza A virus (IAV) host cell infection. We investigated the antiviral activity of the v-ATPase inhibitor saliphenylhalamide (SaliPhe) and compared it with several older v-ATPase inhibitors concanamycin A, bafilomycin A1, (BafA) and archazolid
Konstantin H Müller, Denis E Kainov, Karim El Bakkouri, Xavier Saelens, Jef K De Brabander, Christian Kittel, Elisabeth Samm, Claude P Muller   +7 more
openaire   +2 more sources

Tissue specific expression of the splice variants of the mouse vacuolar proton-translocating ATPase a4 subunit [PDF]

Biochemical and Biophysical Research Communications, 2007
We have identified splicing variants of the mouse a4 subunit which have the same open reading frame but have a different 5'-noncoding sequence. Further determination of the 5'-upstream region of the a4 gene in mouse indicated the presence of two first exons (exon 1a and exon 1b) which include the 5'-noncoding sequence of each variant. The mRNAs of both
Shoko, Kawasaki-Nishi, Akihito, Yamaguchi, Michael, Forgac, Tsuyoshi, Nishi   +3 more
openaire   +2 more sources