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

Hyeonwoo Kim; Hong Zhang; David Meng; Geoffrey Russell; Joon No Lee; Jin Ye

(Profiled Authors: Jin Ye; Hong Zhang)

Journal of Lipid Research. 2013;54(8):2144-2152.


Ubxd8, a multidomain protein sensor for longchain 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. Copyright © 2013 by the American Society for Biochemistry and Molecular Biology, Inc.

PMID: 23720822     PMCID: PMC3708364    

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