A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex

Hirokazu Yagi, Kazuhiro Ishimoto, Takeshi Hiromoto, Hiroaki Fujita, Tsunehiro Mizushima, Yoshinori Uekusa, Maho Yagi-Utsumi, Eiji Kurimoto, Masanori Noda, Susumu Uchiyama, Fuminori Tokunaga, Kazuhiro Iwai, Koichi Kato

Research output: Contribution to journalArticlepeer-review

47 Citations (Scopus)


HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.

Original languageEnglish
Pages (from-to)462-468
Number of pages7
JournalEMBO Reports
Issue number5
Publication statusPublished - 2012 May 1
Externally publishedYes


  • HOIL-1L
  • HOIP
  • NF-kB activation
  • UBA-UBL interaction
  • linear-ubiquitin-chain assembly complex

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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