The interaction of thioredoxin with Txnip. Evidence for formation of a mixed disulfide by disulfide exchange.

ABSTRACT: The thioredoxin system plays an important role in maintaining a reducing environment in the cell. Recently, several thioredoxin binding partners have been identified and proposed to mediate aspects of redox signaling, but the significance of these interactions is unclear in part due to incomplete understanding of the mechanism for thioredoxin binding. Thioredoxin-interacting protein (Txnip) is critical for regulation of glucose metabolism, the only currently known function of which is to bind and inhibit thioredoxin. We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex. We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent wi

SUBMITTER: Patwari P 

PROVIDER: S-EPMC1609191 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature