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ATP6AP1 is somatically mutated in 12% of follicular lymphoma tumors. Mutations clustered around the transmembrane domain.
Experimental investigation of five specific genes, AP3B1 (show AP3B1 ELISA Kits), ATP6AP1, BLOC1S1 (show BLOC1S1 ELISA Kits), LAMP2 (show LAMP2 ELISA Kits), and RAB11A (show RAB11A ELISA Kits), has confirmed novel roles for these proteins in the proper initiation of macroautophagy in amino acid-starved fibroblasts.
The essential role of Ac45 in osteoclast-mediated extracellular acidification and protease exocytosis, as well as the ability of Ac45 to guide lysosomal intracellular trafficking to the ruffled border, is demonstrated.
propose that, in addition to its canonical function in V-ATPase (show ATP6V1H ELISA Kits)-mediated acidification, Ac45 plays versatile roles during osteoclast formation and function.
These results suggest that a3 V-ATPase (show ATP6V1H ELISA Kits) promotes distant metastasis of B16-F10 (show F10 ELISA Kits) cells by creating acidic environments via proton secretion.
Disruption of vacuolar H+-ATPase (show ATP6V1B2 ELISA Kits) a3-B2 subunit interaction inhibited osteoclast bone resorption.
Targeted disruption of the gene for the chromaffin granular V-ATPase (show ATP6V1H ELISA Kits)-associated protein Ac45 in embryonic stem cells affects the normal blastocyst development, suggesting an essential role for the V-ATPase (show ATP6V1H ELISA Kits) in early embryonic development. [AC45]
In osteoclasts, the activity-dependent accumulation of acids and Ca(2 (show CA2 ELISA Kits)+) in the closed extracellular compartment might serve as negative feedback signals for regulating the V-ATPase (show ATP6V1H ELISA Kits).
cytoplasmic terminus of Ac45 contains elements necessary for its proper interaction with V(0) domain and efficient osteoclastic bone resorption
role for furin (show FURIN ELISA Kits) in regulated secretion, particularly in intragranular acidification most likely due to impaired processing of Ac45
This gene encodes a component of a multisubunit enzyme (1 mDa MW) that mediates acidification of eukaryotic intracellular organelles. Vacuolar ATPase (V-ATPase) is comprised of a cytosolic V1 (site of the ATP catalytic site) and a transmembrane V0 domain. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, and receptor-mediated endocytosis. The encoded protein of this gene is approximately 45 kD and may assist in the V-ATPase-mediated acidification of neuroendocrine secretory granules.
ATPase, H+ transporting, lysosomal (vacuolar proton pump), subunit 1
, ATPase, H+ transporting, lysosomal interacting protein 1
, H-ATPase subunit
, V-ATPase Ac45 subunit
, V-ATPase S1 accessory protein
, V-ATPase subunit S1
, V-type proton ATPase subunit S1
, protein XAP-3
, vacuolar proton pump subunit S1
, V-ATPase subunit Ac45
, protein C7-1
, vacuolar H+ ATPase accessory subunit 1