MW 367.40, Purity | 99%. H+ / K+-ATPase (proton pump) inhibitor (IC50 = 2.3 µM). S-enantiomer of omeprazole. Attenuates intestinal mucosal barrier damage and can promote healing of gastric…

The kinetics of the interaction between the V-ATPase subunit (Vph1p) and the Vma12p/Vma22p assembly complex suggest that the interaction may occur only for the duration of the assembly of the membrane sector of the V-ATPase (Vo). According to this model, the Vma12p/ Vma22p assembly complex would release the assembled Vo sector, and the Vo sector and/or assembled V-ATPase complex would be loaded into ER-derived vesicles bound for the Golgi complex. To determine whether Vph1p would continue to associate with the assembly complex in the absence of membrane traffic out of the ER, we used a temperature sensitive allele, sec12-4, to block protein exit from the ER at the restrictive temperature (Nakano et al., 1988). The sec12-4 cells were grown at 23°C before the addition of [35S]methionine, and an aliquot of the cells was shifted to the nonpermissive temperature (37°C for 15 min) to induce the temperature-sensitive block. Cells were radiolabeled for 5 min and chased for various times after the ...

ATP-hydrolysis and proton pumping by the V-ATPase (vacuolar proton-translocating ATPase) are subject to redox regulation in mammals, yeast and plants. Oxidative inhibition of the V-ATPase is ascribed to disulfide-bond formation between conserved cysteine residues at the catalytic site of subunit A. Subunits containing amino acid substitutions of one of three conserved cysteine residues of VHA-A were expressed in a vha-A null mutant background in Arabidopsis. In vitro activity measurements revealed a complete absence of oxidative inhibition in the transgenic line expressing VHA-A C256S, confirming that Cys256 is necessary for redox regulation. In contrast, oxidative inhibition was unaffected in plants expressing VHA-A C279S and VHA-A C535S, indicating that disulfide bridges involving these cysteine residues are not essential for oxidative inhibition. In vivo data suggest that oxidative inhibition might not represent a general regulatory mechanism in plants. ...

Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning V0 domain. Both the multitude of locations and the heteromultimeric structure make it likely that the expression and the activity of V-ATPases are regulated in various ways. Regulation of gene expression encompasses control of transcription as well as control at the post-transcriptional level. Regulation of enzyme activity encompasses many diverse mechanisms such as disassembly/reassembly of V1 and V0 domains, oxidation of SH groups, control by activator and inhibitor proteins or by small signalling molecules, and sorting of the holoenzyme or its subunits to target membranes. ...

Editorial Focus F303-2013 Connecting type A intercalated cell metabolic state to V-ATPase function: phosphorylation does matter! Am J Physiol Renal Physiol. 2013 Jul 31; Authors: Rieg T, Dominguez Rieg JA Abstract none. PMID: 23904225 [PubMed - as supplied by publisher]...

Approaches to Time-Resolved Electron Cryo-Microscopy. Howard White - John Rubinstein Lab, Dept of Biochemistry, Univ of Toronto. Vacoular-type ATPases (V-ATPases) in eukaryotes are ATP-dependent proton pumps that acidify intracellular compartments such as lysosomes, endosomes, and secretory vesicles. V-ATPase is evolutionarily related to the F-type ATP synthase but they differ in subunit composition and arrangement. Both enzymes use a rotary catalytic mechanism where ATP hydrolysis drives rotation of a rotor subcomplex within the enzyme resulting in proton translocation through the membrane-bound Fo or Vo regions. The reaction can also run in the opposite direction during ATP synthesis. In some eubacteria and archaea, V-ATPase functions exclusively as an ATP synthase in order to generate ATP for these organisms. The overall architecture of V-ATPase can be separately into a soluble, catalytic V1 region, a membrane-bound region as well as the peripheral stalks. Here we report the intact structure ...

In this study, we examined the transcript levels and transcriptional activities of several V-ATPase genes of M. sexta larvae during the moult and during periods of starvation, both states in which V-ATPase activity is shut down by reversible disassembly of the holoenzyme (Sumner et al., 1995). The rapid and enormous growth of larvae from hatching to pupation - they increase their body mass within 3 weeks by a factor of approximately 104 - requires that the uptake of nutrients such as amino acids is energized very effectively. For this reason, it is not surprising that 10% of total larval ATP production is spent on active K+ transport in the midgut (Dow and Peacock, 1989), and this is driven by the plasma membrane V-ATPase (Wieczorek et al., 2000). However, high rates of ATP consumption entail strict control of enzyme activity and, since V-ATPase is present in high densities in the goblet cell apical membranes (up to approximately 5000 molecules μm-2), also strict control of its biosynthesis. We ...

Vacuolar-type H+ -ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient. V-ATPases are found within the membranes of many organelles, such as endosomes, lysosomes, and secretory vesicles, where they play a variety of roles crucial for the function of these organelles. For example, the proton gradient across the yeast vacuolar membrane generated by V-ATPases drives calcium uptake into the vacuole through an H+ ...

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.

The vacuolar ATPases (V-ATPases) are a family of proton pumps that couple ATP hydrolysis to proton transport into intracellular compartments and across the plasma membrane. They function in a wide array of normal cellular processes, including membrane traffic, protein processing and degradation, and …

Concanamycin A is the major analogue of the concanamycin complex produced by Streptomyces sp.. It has been shown to act as a potent and specific vacuolar-ATPase inhibitor. Concanamycin A inhibits the acidification of organelles and blocks cell surface expression of viral envelope glycoproteins without affecting their synthesis. It also interferes with intracellular protein trafficking and inhibits perforin- and Fas-based lytic pathways in cell-mediated cytotoxicity. Concanamycins are structurally related to the bafilomycins ...

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c, c, and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene is one of two genes that encode the V1 domain C subunit proteins and is found ubiquitously. This C subunit is analogous but not homologous to gamma subunit of F-ATPases. Previously, this gene was ...

V-type proton ATPase subunit H; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity) (441 aa ...

The membrane sector (Vo) from the proton pumping vacuolar ATPase (V-ATPase V1Vo-ATPase) from was purified to homogeneity and its structure was characterized by EM of single molecules and two-dimensional crystals. V1Vo revealed that the cytoplasmic N-terminal domain of subunit a (aNT) must undergo a large conformational change upon enzyme disassembly or (re)assembly from Vo V1 and subunit C. Isothermal titration calorimetry using recombinant subunit d and aNT revealed that the two proteins bind each other with a of ～5 μm. Treatment of the purified Vo sector with 1-palmitoyl-2-hydroxy-complex. Passive proton translocation assays revealed that both Vo and VoΔare impermeable to protons. We speculate that the structural change in subunit a upon release of V1 from Vo during reversible enzyme dissociation plays a role in blocking passive proton translocation across free Geldanamycin Vo and that Geldanamycin the interaction between aNT and d seen in free Vo functions to stabilize the Vo sector for ...

TY - JOUR. T1 - Palmitate-Induced Vacuolar-Type H(+)-ATPase Inhibition Feeds Forward Into Insulin Resistance and Contractile Dysfunction. AU - Liu, Yilin. AU - Steinbusch, Laura K. M.. AU - Nabben, Miranda. AU - Kapsokalyvas, Dimitris. AU - van Zandvoort, Marc. AU - Schonleitner, Patrick. AU - Antoons, Gudrun. AU - Simons, Peter J.. AU - Coumans, Will A.. AU - Geomini, Amber. AU - Chanda, Dipanjan. AU - Glatz, Jan F. C.. AU - Neumann, Dietbert. AU - Luiken, Joost J. F. P.. PY - 2017/6/1. Y1 - 2017/6/1. KW - FATTY-ACID UPTAKE. KW - CARDIAC MYOCYTES. KW - INDUCED LIPOTOXICITY. KW - LIPID-ACCUMULATION. KW - RATS. KW - METABOLISM. KW - GLUCOSE. KW - CD36. KW - DIET. KW - PROTECTS. U2 - 10.2337/db16-0727. DO - 10.2337/db16-0727. M3 - Article. VL - 66. SP - 1521. EP - 1534. JO - Diabetes. JF - Diabetes. SN - 0012-1797. IS - 6. ER - ...

The F-ATPase in bovine mitochondria is a membrane-bound complex of about 30 subunits of 18 different kinds. Currently, ∼85% of its structure is known. The enzyme has a membrane extrinsic catalytic domain, and a membrane intrinsic domain where the turning of the enzymes rotor is generated from the transmembrane proton-motive force. The domains are linked by central and peripheral stalks. The central stalk and a hydrophobic ring of c-subunits in the membrane domain constitute the enzymes rotor. The external surface of the catalytic domain and membrane subunit a are linked by the peripheral stalk, holding them static relative to the rotor. The membrane domain contains six additional subunits named ATP8, e, f, g, DAPIT (diabetes-associated protein in insulin-sensitive tissues), and 6.8PL (6.8-kDa proteolipid), each with a single predicted transmembrane α-helix, but their orientation and topography are unknown. Mutations in ATP8 uncouple the enzyme and interfere with its assembly, but its roles ...

The |i|a|/i| subunit is the largest of 15 different subunits that make up the vacuolar H|sup|+|/sup|-ATPase (V-ATPase) complex, where it functions in proton translocation. In mammals, this subunit has four paralogous isoforms, |i|a|/i|1-|i|a|/i|4, which may encode signals for targeting assembled V-A …

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Macrophages perform key functions in tissue homeostasis that are influenced by the local tissue environment. Within the tumor microenvironment, tumor-associated macrophages can be altered to acquire properties that enhance tumor growth. Here, we found that lactate, a metabolite found in high concentration within the anaerobic tumor environment, activated mTORC1 that subsequently suppressed TFEB-mediated expression of the macrophage-specific vacuolar ATPase subunit ATP6V0d2. Atp6v0d2-/- mice were more susceptible to tumor growth, with enhanced HIF-2α-mediated VEGF production in macrophages that display a more protumoral phenotype. We found that ATP6V0d2 targeted HIF-2α but not HIF-1α for lysosome-mediated degradation. Blockade of HIF-2α transcriptional activity reversed the susceptibility of Atp6v0d2-/- mice to tumor development. Furthermore, in a cohort of patients with lung adenocarcinoma, expression of ATP6V0d2 and HIF-2α was positively and negatively correlated with survival, ...

Manzamine A is a vacuolar ATPase uncoupler and GSK-3 inhibitor found in marine sponges. It inhibits autophagy and tumor growth in cancer models, suppresses foam cell formation in macrophages, prevents growth of gram positive and gram negative bacteria, and decreases tau hyperphosphorylation.

CRI is driven mainly by cells of the innate immune system, predominantly TAMs (2, 34). Previous reports point to the importance of V-ATPases in tumor progression and migration (6, 8, 35). Other investigators have described the fundamental role of V-ATPase during cytokine trafficking and secretion (36-38). Our studies bridge the gap between these two research areas by showing that a peptide signal of V-ATPase origin participates in the induction of an inflammatory response from monocytes.. We show that incubation of monocytes with a2NTD leads to upregulation of several genes/proteins involved in M2 polarization. a2NTD induces an M2-like phenotype in monocytes (Fig. 2) described as IL-12low, IL-23low, and IL-10high (16). The increased levels of IL-10 correspond to the significant levels of p50 in the nucleus after a2NTD stimulation (Fig. 3D). Whereas p50 homodimers are traditionally associated with transcriptional repression (39), p50 induces IL-10 transcription by binding the IL-10 promoter in ...

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CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core CC - and F(0) - the membrane proton channel. F(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main CC subunits: a(1), b(1), b(1) and c(10-14). The alpha and beta chains CC form an alternating ring which encloses part of the gamma chain. F(1) CC is attached to F(0) by a central stalk formed by the gamma and epsilon CC chains, while a peripheral stalk is formed by the delta, b and b CC chains. else CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core CC - and F(0) - the membrane proton channel. F(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an CC alternating ring which encloses part of the gamma chain. F(1) is CC attached to F(0) by a central stalk formed by the gamma and epsilon CC chains, while a peripheral stalk is formed by the delta ...

In the absence of PLZF, NKT cells do not acquire innate T cell effector functions and do not express activation markers typically expressed by innate-like T cells (24, 25). In this study, we showed that in addition to NKT cells, PLZF is highly expressed by ∼70% of thymic and ∼40% of peripheral Vγ1.1+Vδ6.3+ T cells (Fig. 1, Supplemental Fig. 1). The presence of Vγ1.1+Vδ6.3+ T cells in PLZF-deficient mice and the significant reduction of only the PLZF-expressing Vγ1.1+Vδ6.3+ T cells in SAP-deficient mice strongly suggested that PLZF-positive and -negative Vγ1.1+Vδ6.3+ T cells represent two distinct lineages. Interestingly, the Vγ1.1+Vδ6.3+ iIELs also did not express PLZF, although it is possible that these cells developed extrathymically (57).. PLZF-positive and -negative Vγ1.1+Vδ6.3+ T cells were phenotypically similar. Compared with the other γδ T cell subsets, both populations expressed high levels of CD44, and about half expressed NK1.1. However, the low expression of CD62L ...

V-ATPase F antibody (ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F) for WB. Anti-V-ATPase F pAb (GTX101768) is tested in Human samples. 100% Ab-Assurance.

Negli ultimi anni, diversi studi hanno descritto la presenza di subunità F0F1 ATP sintasi ed è inibitore IF1 sulla superficie cellulare di cellule diverse con il settore catalitico F1 rivolta verso lesterno. Lenzima, chiamato ectopica ATPasi / sintasi, è stato trovato per mediare varie funzioni biologiche quali endocitosi HDL, regolazione pH transmembrana, riconoscimento della cellula tumorale. Una domanda interessante è se lenzima ectopica ha la stessa composizione subunità e massa molecolare come quello della sintasi mitocondriale ATP. Unaltra questione è la sua localizzazione in membrana plasmatica, soprattutto in epatociti causa della loro natura polare, in cui lenzima HDL media endocitosi. Utilizzando diversi metodi per preparare membrane plasmatiche di fegato di ratto, che sono stati sottoposti ad estrazione digitonina, hr CNE, immunoblotting, immunoprecipitazione e spettrometria di massa, la presenza di ectopici F0F1 complessi con un peso molecolare simile alla forma monomerica ...

To understand vesicle refilling and quantal size determinants during ongoing activity, we set out to study synaptic vesicle reacidification kinetics by monitoring the fluorescence of SpH in CNS boutons after trains of APs. By rapidly quenching surface SpH with pressure-pulse applications of acid, we isolated a quench-protected fluorescence signal that reflects reacidification kinetics isolated from distortion by ongoing endocytosis. Surface quenching also eliminates alternate fluorescence decay pathways, such as that which might be caused by lateral diffusion of vesicular SpH from sites of exocytosis into neighboring axon (Sankaranarayanan and Ryan, 2000). A possible artifact of quench experiments could arise from slow access of the acid to surface SpH in tortuous membrane invaginations, posited by some (Wilkinson and Cole, 2001) to arise in the poststimulus period. The complete block of the decay of fluorescence during the quench period by exposure to the V-ATPase inhibitor Baf (Fig. 2) ...

FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This locus represents naturally occurring read-through transcription between the ATP5J2 (ATP synthase, H+ transporting, mitochondrial Fo complex, subunit F2) and PTCD1 (pentatricopeptide repeat domain 1) genes on chromosome 7. The read-through transcript encodes a fusion protein that shares sequence identity with each individual gene product. [provided by RefSeq, Nov 2010 ...

pmes:FX988_01656 K03387 NADH-dependent peroxiredoxin subunit F [EC:1.8.1.-] , (GenBank) NADH dehydrogenase (A) MLDAKLKGQLATYLENLTSQVELRIAVDEQHQAKKSAEISDLANDIAELSPLVKVVAQSK NDVRKPSMEVVSVKNNTSITFAGVPMGHEFTSLVLALLNSGGHPVKISEEQVTEIKALSG SYQFETYVSLSCQTCTGVVQALNVLSVINPNITNTMIDGSLFQDEVNERNIMSVPSVYLN GELFTQGAVTIDKILSKIDPHADAKQAESLNDKDPYDMLIVGGGPAGAAAAIYAARKGIR TGIVAEKFGGQVTDTMAIENFISVKATEGPKLVTGLEQHVKDYNVDIMDNNKAVKLSKDG LINIELENGAMLSSKTVMLATGARWREMNVPGEQQYRGAGVAYCPHCDGPLFKGKRVAVI GGGNSGIEAALDLANIVEHVTVLEFDTKLRADEVLQRKAKAAKNIDIILNAMTTEVLGDG KRVTGLTYQDRVSQESKHVELAGIFVQIGLVPNSEWLKGDIALTPRGEIEVGQRGETSIE GVFAAGDVTTAPYKQIIIAMGDGANAALGAFDYLLRAPSVESANDSEKAA ...

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View mouse Atp6v0d2 Chr4:19876841-19922605 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression

Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...

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The 16 kDa proteolipid (subunit c) of the eukaryotic vacuolar H(+)-ATPase (V-ATPase) is closely related to the ductin polypeptide that forms the connexon channel of gap junctions in the crustacean Nephrops norvegicus. Here we show that the major protein component of Manduca sexta gap junction preparations is a 16 kDa polypeptide whose N-terminal sequence is homologous to ductin and is identical to the deduced sequence of a previously cloned cDNA from Manduca (Dow et al., Gene, 122, 355-360, 1992). We also show that a Drosophila melanogaster cDNA, highly homologous to the Manduca cDNA, can rescue Saccharomyces cerevisiae, defective in V-ATPase function, in which the corresponding yeast gene, VMA3, has been inactivated. Evidence is presented for a single genetic locus (Vha16) in Drosophila, which in adults at least contains a single transcriptional unit. Taken together, the data suggest that in Drosophila and Manduca, the same polypeptide is both the proteolipid subunit c component of the V-ATPase and the

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n animal regeneration, control of position-dependent cell proliferation is crucial for the complete restoration of patterned appendages in terms of both, shape and size. However, detailed mechanisms of this process are largely unknown. In this study, we identified leucine/glutamine and v-ATPase/lysosomal acidification, via mechanistic target of rapamycin complex 1 (mTORC1) activation, as effectors of amputation plane-dependent zebrafish caudal fin regeneration. mTORC1 activation, which functions in cell proliferation, was regulated by lysosomal acidification possibly via v-ATPase activity at 3 h post amputation (hpa). Inhibition of lysosomal acidification resulted in reduced growth factor-related gene expression and suppression of blastema formation at 24 and 48 hpa, respectively. Along the proximal-distal axis, position-dependent lysosomal acidification and mTORC1 activation were observed from 3 hpa. We also report that Slc7a5 (L-type amino acid transporter), whose gene expression is ...

TY - JOUR. T1 - Isolation and reconstitution of a vacuolar-type proton pump of osteoclast membranes. AU - Mattsson, Jan P.. AU - Schlesinger, Paul H.. AU - Keeling, David J.. AU - Teitelbaum, Steven L.. AU - Stone, Dennis K.. AU - Xie, Xiao Song. N1 - Copyright: Copyright 2014 Elsevier B.V., All rights reserved.. PY - 1994/10/7. Y1 - 1994/10/7. N2 - A vacuolar-type proton-translocating ATPase was extracted from ruffled membranes of chicken osteoclasts with 1% polyoxyethylene 9-lauryl ether (C12E9) and was purified 13-fold by glycerol gradient centrifugation. The isolated pump appears by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to have a subunit composition similar to that of the clathrin-coated vesicle proton pump, in that subunits of apparent molecular masses of 116, 71, 57, 40, 39, 33, and 17 kDa are present in the osteoclast pump preparation. In addition, the 116-, 71-, 57-, and 40-kDa components were shown to cross-react with specific antisera generated against the ...

The present work was aimed at characterizing the process of cell entry of the anthrax EF and of the modification of the concentration and distribution of cAMP that EF induces in living cells. These goals were reached by using fluorescent PKA‐based probes for optical imaging of cAMP with subcellular spatial resolution and appropriate biochemical assays. An important finding presented here is that EF reaches its cytosolic substrate ATP with a time course, determined with both biochemical and imaging assays, similar to that of the anthrax LF. LF was previously shown to enter the cytosol via the endocytic route at the late endosomal stage (Abrami et al, 2005). Similarly to LF, EF entry depends strictly on the activity of the vacuolar ATPase proton pump; the effect of its specific inhibitor bafilomycin A1, added at different time periods after the toxin, also indicates a sorting out of EF from late endosomes. Taken together, these results provide strong evidence that EF is endocytosed together with ...

article{8509671, abstract = {Defects of the V-type proton (H+) ATPase (V-ATPase) impair acidification and intracellular trafficking of membrane-enclosed compartments, including secretory granules, endosomes, and lysosomes. Whole-exome sequencing in five families affected by mild to severe cutis laxa, dysmorphic facial features, and cardiopulmonary involvement identified biallelic missense mutations in ATP6V1E1 and ATP6V1A, which encode the El and A subunits, respectively, of the V-1 domain of the heteromultimeric V-ATPase complex. Structural modeling indicated that all substitutions affect critical residues and inter- or intrasubunit interactions. Furthermore, complexome profiling, a method combining blue-native gel electrophoresis and liquid chromatography tandem mass spectrometry, showed that they disturb either the assembly or the stability of the V-ATPase complex. Protein glycosylation was variably affected. Abnormal vesicular trafficking was evidenced by delayed retrograde transport after ...

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

The spontaneous mouse grey-lethal (gl) mutation is responsible for a coat color defect and for the development of the most severe autosomal recessive form of osteopetrosis. Using a positional cloning approach, we have mapped and isolated the gl locus

Recent evidence suggests that the route and rate of Notch traffic through endocytic compartments can be regulated to either potentiate or diminish signaling activity. Our results identify a physiological mechanism to account for this effect on signaling. We identify a set of genes required for endosomal Notch signaling that encode subunits of the V-ATPase, the molecular machine that creates a proton motive force to acidify most compartments of the endosomal system. The data thus establish a novel role of V-ATPase that is relevant to both physiological and pathological Notch signaling. While this work was under review, an article describing a similar role for V-ATPase regulators and a different subunit of the V-ATPase in Notch signaling was published (Yan et al., 2009). Our independent results confirm those findings and expand them by reporting the ultrastructure of V-ATPase mutant cells, extending the role to tumor contexts that depend on excess Notch signaling activity and, importantly, ...

Bone resorption relies on the extracellular acidification function of V-ATPase (vacuolar-type proton-translocating ATPase) proton pump(s) present in the plasma membrane of osteoclasts. The exact configuration of the osteoclast-specific ruffled border V-ATPases remains largely unknown. In the present study, we found that the V-ATPase subunit Atp6v1c1 (C1) is highly expressed in osteoclasts, whereas subunits Atp6v1c2a (C2a) and Atp6v1c2b (C2b) are not. The expression level of C1 is highly induced by RANKL [receptor activator for NF-κB (nuclear factor κB) ligand] during osteoclast differentiation; C1 interacts with Atp6v0a3 (a3) and is mainly localized on the ruffled border of activated osteoclasts. The results of the present study show for the first time that C1-silencing by lentivirus-mediated RNA interference severely impaired osteoclast acidification activity and bone resorption, whereas cell differentiation did not appear to be affected, which is similar to a3 silencing. The F-actin ...

Vacuolar ATP synthase subunit H (EC 3.6.3.14) (V-ATPase H subunit) (Vacuolar proton pump subunit H) (V-ATPase 50/57 kDa subunits) (Vacuolar proton pump subunit SFD) (VMA13) (Nef-binding protein 1) (NBP1). [Source:Uniprot/SWISSPROT;Acc:Q9UI12 ...

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c, c, and d. This gene is one of four genes in man and mouse that encode different isoforms of the a subunit. Alternatively spliced transcript variants encoding the same protein have been described. Mutations in this gene are associated with renal tubular acidosis associated with preserved hearing. [provided by RefSeq, Jul 2008] ...

vacuolar ATP synthase subunit B, putative / V-ATPase B subunit, putative / vacuolar proton pump B subunit, putative / V-ATPase 57 kDa subunit, putative; FUNCTIONS IN: hydrogen ion transporting ATP synthase activity, rotational mechanism, hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances, proton-transporting ATPase activity, rotational mechanism; INVOLVED IN: proton transport, ATP metabolic process, ATP synthesis coupled proton transport; LOCATED IN: plasma membrane, vacuole, membrane, chloroplast envelope; EXPRESSED IN: 27 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal (InterPro:IPR000793), ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal (InterPro:IPR004100), ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding (InterPro:IPR000194), ATPase, V1 complex, subunit B (InterPro:IPR005723); BEST Arabidopsis thaliana protein match is: vacuolar ATP ...

Another link between apoptosis and mitochondrial physiology is suggested by the presence of Bcl-2 family proteins in mitochondrial membranes (42). The Caenorhabditis elegans Bcl-2 homolog CED-9 is expressed from a bicistronic mRNA that encodes both CED-9 and cytochrome b (43). This suggests a functional connection between Bcl-2 family proteins and these organelles and implies that CED-9 may have originated from the genome of protomitochondrial symbionts, transferred along with other mitochondrial genes to the nuclear genome.. Many (but not all) Bcl-2 family proteins reside in the mitochondrial outer membrane, anchored by a hydrophobic stretch of amino acids located within their COOH-termini, with the proteins orientated toward the cytosol (42). A wide variety of mitochondrial events have been reported to be modulated by Bcl-2 and its homologs. These include some that directly affect mitochondria such as oligomycin, which inhibits the F0F1-adenosine triphosphatase (ATPase) proton pump of the ...

Recent publications:. Anne Kriegel, Zaida Andrés, Anna Medzihradszky, Falco Krüger, Stefan Scholl, Simon Delang, M. Görkem Patir-Nebioglu, Gezahegn Gute, Haibing Yang, Angus S. Murphy, Wendy Ann Peer, Anne Pfeiffer, Melanie Krebs, Jan U. Lohmann and Karin Schumacher (2015) Job Sharing in the Endomembrane System: Vacuolar Acidification Requires the Combined Activity of V-ATPase and V-PPase. Plant Cell, doi: 10.1105/tpc.15.00733. Yu Luo, Stefan Scholl, Anett Doering, Yi Zhang, Niloufer G. Irani, Simone Di Rubbo, Lutz Neumetzler, Praveen Krishnamoorthy, Isabelle Van Houtte, Evelien Mylle, Volker Bischoff, Samantha Vernhettes, Johan Winne, Jirí Friml, York-Dieter Stierhof, Karin Schumacher, Staffan Persson & Eugenia Russinova (2015) V-ATPase activity in the TGN/EE is required for exocytosis and recycling in Arabidopsis. Nature Plants 1, Article number: 15094, doi:10.1038/nplants.2015.94. Keinath NF, Waadt R, Brugman R, Schroeder JI, Grossmann G, Schumacher K, Krebs M. (2015) Live Cell Imaging ...

The nascent phagosome is not inherently bactericidal. As it matures, it becomes more acidic from pH 6.5 to pH 4, and gains characteristic protein markers and hydrolytic enzymes. The different enzymes function at various optimal pH, forming a range so they each work in narrow stages of the maturation process. Enzyme activity can be fine-tuned by modifying the pH level, allowing for greater flexibility. The phagosome moves along microtubules of the cytoskeleton, fusing with endosomes and lysosomes sequentially in a dynamic kiss-and-run manner.[15] This intracellular transport depends on the size of the phagosomes. Larger organelles (with a diameter of about 3 µm) are transported very persistently from the cell periphery towards the perinuclear region whereas smaller organelles (with a diameter of about 1 µm) are transported more bidirectionally back and forth between cell center and cell periphery.[16] Vacuolar proton pumps (v-ATPase) are delivered to the phagosome to acidify the organelle ...

About Reverse Osmosis MembranesReverse Osmosis is a technology that uses a semi-permeable membrane to remove dissolved salts or organic molecules. The water is pushed ...

The lack or complexity of high resolution technologies and the need for labelled compound derivatives represents a major limitation on the study of intracellular distribution dynamics of pharmacological agents. The intrinsic, label-free and organelle-specific fluorescence activity of nintedanib presented in this study provides a powerful tool to dissect intracellular accumulation and distribution dynamics of this clinically approved small molecule TKI. The observation that lysosomal alkalization via V-ATPase inhibition sensitized lung cancer cells towards nintedanib suggests that protonation-based lysosomal sequestration represents a cell-intrinsic protection mechanism against this FGFR inhibitor. In accordance, various chemotherapeutic agents including doxorubicin, mitoxantrone and vincristine but also TKIs such as gefitinib, lapatinib and sunitinib have been reported to be subject to inactivating lysosomal sequestration [23, 30]. Together, these findings support a yet underestimated central ...

ID C5M0K1_PERM5 Unreviewed; 343 AA. AC C5M0K1; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256,RuleBase:RU361189}; DE Flags: Fragment; GN ORFNames=Pmar_PMAR001829 {ECO:0000313,EMBL:EEQ97491.1}; OS Perkinsus marinus (strain ATCC 50983 / TXsc). OC Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus. OX NCBI_TaxID=423536 {ECO:0000313,Proteomes:UP000007800}; RN [1] {ECO:0000313,EMBL:EEQ97491.1, ECO:0000313,Proteomes:UP000007800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50983 / TXsc {ECO:0000313,Proteomes:UP000007800}; RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential component of the vacuolar proton pump (V- CC ATPase), a multimeric enzyme that catalyzes the translocation of CC protons across the membranes. Required for ...

BioAssay record AID 602197 submitted by NMMLSC: Small Molecules that Regulate V-ATPase Proton Transport in Yeast using pHLuorin, Single Point, Cherry Pick 2.

Staphylococcus aureus; strain: Newman; locus tag: NWMN_1927 (NWMN_RS11120); symbol: lukG; product: leukocidin/hemolysin toxin subunit F

1.1.008. Proton or Sodium translocating F-type, V-type and A-type ATPases (1 family) 3.A.2 (TCDB) PF00137, PDBsum (27 proteins ...

VMA4 SGDID:S000005859, Chr XV from 943651-944352, Verified ORF, Subunit E of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane ...

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Larva: feeds on the seeds from beneath a dense silken tube fixed against the central stalk of a seedhead from September to March. The larva cuts an elongate hole in the stem and spins a dense but very thin cocoon in the stem, usually just below the seed-head, for pupation from March to early May.. Adult: can be disturbed amongst the foodplant during the day, its small size and shape being reminiscent of a Coleophorid.. ...

Subunit c deposits co-localize with Lamp 1 in homozygous CbCln3Δex7/8 and CbCln6nclf cells.A. Representative micrographs of confluency aged wild-type, CbCln3Δ

ZOBRAZOVACÍ METODY V LÉKAŘSTVÍ Imaging Methods in Medicine MUDr. Tomáš Belšan, CSc. Radiodiagnostické oddělení ÚVN Praha U Vojenské nemocnice 1200, Praha 6 tel.: fax:

View mouse Atp6v0c Chr17:24163866-24169702 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression

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