Vacuolar-type ATPase: A proton pump to lysosomal trafficking.
V-ATPase
lysosome
osteoclast
plasma membrane
secretion
subunit isoform
Journal
Proceedings of the Japan Academy. Series B, Physical and biological sciences
ISSN: 1349-2896
Titre abrégé: Proc Jpn Acad Ser B Phys Biol Sci
Pays: Japan
ID NLM: 9318162
Informations de publication
Date de publication:
2019
2019
Historique:
entrez:
14
6
2019
pubmed:
14
6
2019
medline:
23
11
2019
Statut:
ppublish
Résumé
Vacuolar-type ATPase (V-ATPase), initially identified in yeast and plant vacuoles, pumps protons into the lumen of organelles coupled with ATP hydrolysis. The mammalian counterpart is found ubiquitously in endomembrane organelles and the plasma membrane of specialized cells such as osteoclasts. V-ATPase is also present in unique organelles such as insulin secretory granules, neural synaptic vesicles, and acrosomes of spermatozoa. Consistent with its diverse physiological roles and unique localization, the seven subunits of V-ATPase have 2-4 isoforms that are organelle- or cell-specific. Subunits of the enzyme function in trafficking organelles and vesicles by interacting with small molecule GTPases. During osteoclast differentiation, one of the four isoforms of subunit a, a3, is indispensable for secretory lysosome trafficking to the plasma membrane. Diseases such as osteopetrosis, renal acidosis, and hearing loss are related to V-ATPase isoforms. In addition to its role as an enzyme, V-ATPase has versatile physiological roles in eukaryotic cells.
Identifiants
pubmed: 31189779
doi: 10.2183/pjab.95.018
pmc: PMC6751294
doi:
Substances chimiques
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
261-277Références
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