AI Article Synopsis
- Copper is a crucial micronutrient for oxygen-dependent enzymes but can be toxic in excess, creating a balance that is managed by chaperones and membrane transporters.
- The transporters ATP7A and ATP7B play a key role in regulating copper levels by either exporting it from cells or directing it to the endomembrane system.
- Genetic mutations in ATP7A and ATP7B, similar to those affecting trafficking complexes like retromer and AP-1, can lead to neuropsychiatric disorders due to copper imbalance from improperly located transporters.
Article Abstract
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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6726579 | PMC |
| http://dx.doi.org/10.1016/j.ceb.2019.02.009 | DOI Listing |
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