New wine in old bottles: current progress on P5 ATPases.
P5 ATPases
endoplasmic reticulum
mitochondria
quality control
topogenesis
translocation
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
12 2022
12 2022
Historique:
revised:
19
07
2021
received:
05
04
2021
accepted:
26
08
2021
pubmed:
28
8
2021
medline:
15
12
2022
entrez:
27
8
2021
Statut:
ppublish
Résumé
P5 ATPases are evolutionarily conserved P-type transporters. Despite their important roles in the endoplasmic reticulum (ER) and in lysosomes, the substrate specificities and transporting mechanisms of P5 ATPases have remained mysterious. Recently, several studies have provided genetic, biochemical, and structural evidence to help elucidate the physiological functions and substrates of P5 ATPases. Here, we summarize this progress and discuss the potential transport mechanisms of the P5 ATPases-in particular, P5A ATPase-for further study.
Substances chimiques
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7304-7313Informations de copyright
© 2021 Federation of European Biochemical Societies.
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