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

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2144-2152
Number of pages9
JournalJournal of lipid research
Volume54
Issue number8
DOIs
StatePublished - Aug 2013

Keywords

  • Fas-associated factor 1
  • Insig-1
  • Protein degradation

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology

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