Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-53009
Mol Cell Endocrinol 2017 Mar 05;443:163-174. doi: 10.1016/j.mce.2017.01.024.
Show Gene links Show Anatomy links

Molecular features of the L-type amino acid transporter 2 determine different import and export profiles for thyroid hormones and amino acids.

Hinz KM , Neef D , Rutz C , Furkert J , Köhrle J , Schülein R , Krause G .


???displayArticle.abstract???
The L-type amino acid transporter 2 (LAT2) imports amino acids (AA) and also certain thyroid hormones (TH), e.g. 3,3'-T2 and T3, but not rT3 and T4. We utilized LAT2 mutations (Y130A, N133S, F242W) that increase 3,3'-T2 import and focus here on import and export capacity for AA, T4, T3, BCH and derivatives thereof to delineate molecular features. Transport studies and analysis of competitive inhibition of import by radiolabelled TH and AA were performed in Xenopus laevis oocytes. Only Y130A, a pocket widening mutation, enabled import for T4 and increased it for T3. Mutant F242W showed increased 3,3'-T2 import but no import rates for other TH derivatives. No export was detected for any TH by LAT2-wild type (WT). Mutations Y130A and N133S enabled only the export of 3,3'-T2, while N133S also increased AA export. Thus, distinct molecular LAT2-features determine bidirectional AA transport but only an unidirectional 3,3'-T2 and T3 import.

???displayArticle.pubmedLink??? 28108384
???displayArticle.link??? Mol Cell Endocrinol


Species referenced: Xenopus laevis
Genes referenced: slc7a8