UAS domain of Ubxd8 and FAF1 polymerizes upon interaction with long-chain unsaturated fatty acids.

Ubxd8, a multidomain protein sensor for long-chain unsaturated fatty acids (FAs), plays a crucial role to maintain cellular homeostasis of FAs. Ubxd8 polymerizes upon interaction with long-chain unsaturated FAs, but the molecular mechanism involved in this polymerization remains unclear. Here we report that the UAS domain of Ubxd8 mediates this ...
polymerization. We show that a positively charged surface area in the domain is required for the reaction. Mutations changing the positively charged residues in this area to glutamates prevented long-chain unsaturated FAs from inducing oligomerization of Ubxd8. Consequently, the mutant protein no longer responded to regulation by long-chain unsaturated FAs in cultured cells. Long-chain unsaturated FAs also induced polymerization of Fas-associated factor 1 (FAF1), the only other mammalian protein that contains a UAS domain homologous to that of Ubxd8. These results provide further insights into protein-FA interactions by identifying the UAS domain as a motif interacting with long-chain unsaturated FAs.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Animals, Blood Proteins, CHO Cells, Cells, Cultured, Cricetulus, Fatty Acids, Unsaturated, Humans, Membrane Proteins, Models, Molecular, Polymerization, Protein Structure, Tertiary
J. Lipid Res.
Date: Aug. 01, 2013
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