Structural comparison of the vacuolar and Golgi V-ATPases from
STV1
V-ATPase
VPH1
cryo-EM
membrane protein
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
09 04 2019
09 04 2019
Historique:
pubmed:
27
3
2019
medline:
27
3
2019
entrez:
27
3
2019
Statut:
ppublish
Résumé
Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast
Identifiants
pubmed: 30910982
pii: 1814818116
doi: 10.1073/pnas.1814818116
pmc: PMC6462096
doi:
Banques de données
PDB
['6O7T', '6O7X']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
7272-7277Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : CIHR
ID : MOP81294
Pays : Canada
Organisme : Wellcome Trust
ID : 104633/Z/14/Z
Pays : United Kingdom
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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