Human copper transporter ATP7B (Wilson disease protein) forms stable dimers in vitro and in cells.

ABSTRACT: ATP7B is a copper-transporting P_1B-type ATPase (Cu-ATPase) with an essential role in human physiology. Mutations in ATP7B cause the potentially fatal Wilson disease, and changes in ATP7B expression are observed in several cancers. Despite its physiologic importance, the biochemical information about ATP7B remains limited because of a complex multidomain organization of the protein. By analogy with the better characterized prokaryotic Cu-ATPases, ATP7B is assumed to be a single-chain monomer. We show that in eukaryotic cells, human ATP7B forms dimers that can be purified following solubilization. Deletion of the four N-terminal metal-binding domains, characteristic for human ATP7B, does not disrupt dimerization, i.e. the dimer interface is formed by the domains that are co

SUBMITTER: Jayakanthan S 

PROVIDER: S-EPMC5704462 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature