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

• DOI: 10.1194/jlr.m037218
• Publication Date: 2013-05-30T03:19:00Z
• Authors: Hyeonwoo Kim; Hong Zhang; David Meng; Geoffrey Russell; Joon No Lee; Jin Ye
• Keywords: Unsaturated fatty acid

Ubxd8, a multidomain protein sensor for long-chain unsaturated fatty acids (FAs), plays crucial role to maintain cellular homeostasis of FAs. Ubxd8 polymerizes upon interaction with FAs, but the molecular mechanism involved in this polymerization remains unclear. Here we report that UAS domain mediates polymerization. We show positively charged surface area is required reaction. Mutations changing residues glutamates prevented FAs from inducing oligomerization Ubxd8. Consequently, mutant no longer responded regulation by cultured cells. Long-chain also induced Fas-associated factor 1 (FAF1), only other mammalian contains homologous These results provide further insights into protein-FA interactions identifying as motif interacting