Change search
ReferencesLink to record
Permanent link

Direct link
Unresolved questions in human copper pump mechanisms
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2015 (English)In: Quarterly reviews of biophysics (Print), ISSN 0033-5835, E-ISSN 1469-8994, Vol. 48, no 4, 471-478 p.Article, review/survey (Refereed) Published
Abstract [en]

Copper (Cu) is an essential transition metal providing activity to key enzymes in the human body. To regulate the levels and avoid toxicity, cells have developed elaborate systems for loading these enzymes with Cu. Most Cu-dependent enzymes obtain the metal from the membrane-bound Cu pumps ATP7A/B in the Golgi network. ATP7A/B receives Cu from the cytoplasmic Cu chaperone Atox1 that acts as the cytoplasmic shuttle between the cell membrane Cu importer, Ctr1 and ATP7A/B. Biological, genetic and structural efforts have provided a tremendous amount of information for how the proteins in this pathway work. Nonetheless, basic mechanistic-biophysical questions (such as how and where ATP7A/B receives Cu, how ATP7A/B conformational changes and domain-domain interactions facilitate Cu movement through the membrane, and, finally, how target polypeptides are loaded with Cu in the Golgi) remain elusive. In this perspective, unresolved inquiries regarding ATP7A/B mechanism will be highlighted. The answers are important from a fundamental view, since mechanistic aspects may be common to other metal transport systems, and for medical purposes, since many diseases appear related to Cu transport dysregulation.

Place, publisher, year, edition, pages
2015. Vol. 48, no 4, 471-478 p.
Keyword [en]
copper transport, copperchaperone, Wilson disease protein, Menke's disease protein, ceruloplasmin, biophysical methods
National Category
URN: urn:nbn:se:umu:diva-112265DOI: 10.1017/S0033583515000128ISI: 000364764300012PubMedID: 26537407OAI: diva2:877722
Available from: 2015-12-07 Created: 2015-12-04 Last updated: 2015-12-07Bibliographically approved

Open Access in DiVA

fulltext(474 kB)18 downloads
File information
File name FULLTEXT01.pdfFile size 474 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Wittung-Stafshede, Pernilla
By organisation
Department of Chemistry
In the same journal
Quarterly reviews of biophysics (Print)

Search outside of DiVA

GoogleGoogle Scholar
Total: 18 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 40 hits
ReferencesLink to record
Permanent link

Direct link