Trafficking mechanisms of P-type ATPase copper transporters.
Journal
Current opinion in cell biology
ISSN: 1879-0410
Titre abrégé: Curr Opin Cell Biol
Pays: England
ID NLM: 8913428
Informations de publication
Date de publication:
08 2019
08 2019
Historique:
received:
14
12
2018
revised:
13
02
2019
accepted:
26
02
2019
pubmed:
1
4
2019
medline:
2
4
2020
entrez:
1
4
2019
Statut:
ppublish
Résumé
Copper is an essential micronutrient required for oxygen-dependent enzymes, yet excess of the metal is a toxicant. The tug-of-war between these copper activities is balanced by chaperones and membrane transporters, which control copper distribution and availability. The P-type ATPase transporters, ATP7A and ATP7B, regulate cytoplasmic copper by pumping copper out of cells or into the endomembrane system. Mutations in ATP7A and ATP7B cause diseases that share neuropsychiatric phenotypes, which are similar to phenotypes observed in mutations affecting cytoplasmic trafficking complexes required for ATP7A/B dynamics. Here, we discuss evidence indicating that phenotypes associated to genetic defects in trafficking complexes, such as retromer and the adaptor complex AP-1, result in part from copper dyshomeostasis due to mislocalized ATP7A and ATP7B.
Identifiants
pubmed: 30928671
pii: S0955-0674(18)30130-3
doi: 10.1016/j.ceb.2019.02.009
pmc: PMC6726579
mid: NIHMS1523351
pii:
doi:
Substances chimiques
Copper Transport Proteins
0
Copper-Transporting ATPases
EC 7.2.2.8
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
24-33Subventions
Organisme : NIGMS NIH HHS
ID : K12 GM000680
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM067169
Pays : United States
Organisme : NIAMS NIH HHS
ID : R15 AR070505
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG060285
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.
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