Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1

Jin Sue Song, Kyu Park Joon, Jae Jin Lee, Yun Seok Choi, Kyoung Seok Ryu, Jae Hong Kim, Eunhee Kim, Kong Joo Lee, Young Ho Jeon, Eunice Eun Kyong Kim

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Fas-associated factor (FAF)-1 is a multidomain protein that was first identified as a member of the Fas death-inducing signaling complex, but later found to be involved in various biological processes. Although the exact mechanisms are not clear, FAF1 seems to play an important role in cancer, asbestos-induced mesotheliomas, and Parkinson's disease. It interacts with polyubiquitinated proteins, Hsp70, and p97/VCP (valosin-containing protein), in addition to the proteins of the Fas-signaling pathway. We have determined the crystal structure of the ubiquitin-associated domain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin and ubiquitin-like proteins using nuclear magnetic resonance. hFAF1-UBA revealed a canonical three-helical bundle that selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1 (small ubiquitin-related modifier 1) or NEDD8 (neural precursor cell expressed, developmentally down-regulated 8). The interaction between hFAF1-UBA and di-ubiquitin involves hydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These results provide structural insight into the mechanism of polyubiquitin recognition by hFAF1-UBA. Published by Wiley-Blackwell.

Original languageEnglish
Pages (from-to)2265-2276
Number of pages12
JournalProtein Science
Issue number11
Publication statusPublished - 2009 Nov

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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