Session: OR34-Molecular Mechanisms in Thyroid Hormone Action & Cancer
Room 103 (Moscone Center)
For 14 different MCT8-mutants we performed a Sandwich ELISA approach to study dimerization in comparison to wild type. It was assumed that potentially variations of MCT8 that affect amino acid side-chains oriented to the protein surface might interrupt putative MCT8-MCT8 interface contacts. Surprisingly, we found that exclusively mutations at five residues located directly inside the central transport channel cavity lead to a decrease of MCT8 oligomerization (dimer-separation). In contrast, only mutations (insertion, deletion, substitution) at the membrane spanning helix 2 cause enhanced dimerization capacities and a shift towards higher order complexes.
In conclusion, we here provide first structural information related to MCT8 oligomerization and conclude a causality between oligomerization, transport-mechanisms and particular structural features. These results might be helpful for a closer understanding of T3-transport and also related dysfunctionalities, which might be also important for other members of the MFS.
Nothing to Disclose: JF, GK, AG, HK, HB
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