Human bile acid transporter ASBT (SLC10A2) forms functional non-covalent homodimers and higher order oligomers.

ABSTRACT: The human apical sodium-dependent bile acid transporter, hASBT/SLC10A2, plays a central role in cholesterol homeostasis via the efficient reabsorption of bile acids from the distal ileum. hASBT has been shown to self-associate in higher order complexes, but while the functional role of endogenous cysteines has been reported, their implication in the oligomerization of hASBT remains unresolved. Here, we determined the self-association architecture of hASBT by site-directed mutagenesis combined with biochemical, immunological and functional approaches. We generated a cysteine-less form of hASBT by creating point mutations at all 13 endogenous cysteines in a stepwise manner. Although Cysless hASBT had significantly reduced function correlated with lowered surface expression, it featured an ex

SUBMITTER: Chothe PP 

PROVIDER: S-EPMC5780253 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature