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We report biallelic mutations in ATP6V1E1 and ATP6V1A (show ATP6V1A Proteins), respectively encoding the E1 and A subunits of the V1 domain of V-ATPase (show ATP6V1H Proteins), as a cause of distinct metabolic and multisystemic cutis laxa entities.
Low-grade PanIN lesions with typical columnar morphology displayed diffuse labeling of the V1E subunit. In advanced lesions it was (show ATP6V1H Proteins) found along t (show WNT2 Proteins)he basolatera (show CTNNB1 Proteins)l membranes.
The genes CECR2, SLC25A18 and ATP6V1E1, mapping within the critical region for cat eye syndrome (CES), may be responsible for anorectal, renal and preauricular anomalies in patients with CES.
Data demonstrate the physiological significance of the interaction between the E and H subunits of V-ATPase (show ATP6V1H Proteins) and extend previous studies on the arrangement of subunits on the peripheral stalk of V-ATPase (show ATP6V1H Proteins).
there is an important role for physical association between aldolase and the A, B and E subunits of V-ATPase (show ATP6V1H Proteins) in the regulation of the proton pump
HuR (show ELAVL1 Proteins) shows increased binding to some V-ATPase (show ATP6V1H Proteins) mRNAs during ATP depletion; siRNA-mediated knockdown of HuR (show ELAVL1 Proteins) results in diminished V-ATPase (show ATP6V1H Proteins) expression
Rat vacuolar H(+)ATPase (show ATP6V1B2 Proteins) associates with NHE-RF (Na(+)/H(+) exchanger regulatory factor); the E subunit was co-immunoprecipitated from rat kidney cytosol with NHE-RF antibodies.
The mouse V-ATPase E may participate in the regulation of the mSos1-dependent Rac1 signaling pathway involved in growth factor receptor (show RYK Proteins)-mediated cell growth control.
In pancreatic intraepithelial lesions, V1E subunits localized to the basolateral domain in specific regions. Blocking the v-ATPase (show ATP6V1H Proteins) disrupted Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling in primary PanIN cells.
These results suggest that the B1 vacuolar H(+)-ATPase (show ATP6V1B2 Proteins) subunit (show ATP6AP1 Proteins) is necessary for the furosemide-induced acute urinary acidification.
These results suggest that subunit E, especially its amino-terminal domain, plays a pertinent role in the assembly of V-ATPase (show ATP6V1H Proteins) subunits in vacuolar membranes from mice and yeast.
A cDNA encoding a novel putative neuron-specific isoform of vacuolar proton-translocating ATPase (V-ATPase), NM9.2, was isolated from rat and mouse.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle 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 encoded protein is possibly part of the V0 subunit. Since two nontranscribed pseudogenes have been found in dog, it is possible that the localization to chromosome 2 for this gene by radiation hybrid mapping is representing a pseudogene. Genomic mapping puts the chromosomal location on 5q35.3.
V-type proton ATPase subunit E 1
, ATPase, H+ transporting, vacuolar, V1 subunit E
, V-type proton ATPase subunit e 1
, v-type proton ATPase subunit e 1
, H(+)-transporting two-sector ATPase, 31kDa subunit
, H+-transporting ATP synthase chain E, vacuolar
, V-ATPase 31 kDa subunit
, V-ATPase subunit E 1
, V-ATPase, subunit E
, vacuolar proton pump subunit E 1
, vacuolar H+ ATPase E1
, ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e
, V-ATPase 9.2 kDa membrane accessory protein
, V-ATPase M9.2 subunit
, vacuolar proton pump subunit e 1
, V-ATPase subunit e 1
, Vacuolar ATP synthase subunit e 1
, vacuolar proton-ATPase subunit ATP6H
, H(+)-transporting two-sector ATPase, subunit H
, V-ATPase H subunit
, vacuolar ATP synthase subunit H
, vacuolar proton pump H subunit
, vacuolar proton-ATPase subunit M9.2
, ATPase, H+ transporting lysosomal (vacuolar proton pump), 9.2 kDa
, ATPase, H+ transporting, V0 subunit e
, ATPase, H+ transporting, lysosomal 9kD V0 subunit E
, lysosomal 9kDa
, ATPase, H+ transporting lysosomal (vacuolar proton pump), 32 kDa
, ATPase, H+ transporting, V1 subunit E
, ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E
, H(+)-ATPase E-like protein
, H+ ATPase subunit E
, VATPase, H+ transporting, lysosomal V1 subunit E1
, lysosomal 31kDa
, vacuolar H(+)-ATPase, E subunit
, ATPase, H+ transporting, V0 subunit E
, ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1
, ATPase, H+ transporting, lysosomal V0 subunit E1
, D-serine-regulated transcript 1 protein