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 journalArticle

35 Citations (Scopus)

Abstract

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
Volume13
Issue number5
DOIs
Publication statusPublished - 2012 May 1
Externally publishedYes

Fingerprint

Ubiquitin
Chemical activation
Ubiquitin-Protein Ligases
Proteins

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Biochemistry

Cite this

Yagi, H., Ishimoto, K., Hiromoto, T., Fujita, H., Mizushima, T., Uekusa, Y., ... Kato, K. (2012). A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex. EMBO Reports, 13(5), 462-468. https://doi.org/10.1038/embor.2012.24

A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex. / Yagi, Hirokazu; Ishimoto, Kazuhiro; Hiromoto, Takeshi; Fujita, Hiroaki; Mizushima, Tsunehiro; Uekusa, Yoshinori; Yagi-Utsumi, Maho; Kurimoto, Eiji; Noda, Masanori; Uchiyama, Susumu; Tokunaga, Fuminori; Iwai, Kazuhiro; Kato, Koichi.

In: EMBO Reports, Vol. 13, No. 5, 01.05.2012, p. 462-468.

Research output: Contribution to journalArticle

Yagi, H, Ishimoto, K, Hiromoto, T, Fujita, H, Mizushima, T, Uekusa, Y, Yagi-Utsumi, M, Kurimoto, E, Noda, M, Uchiyama, S, Tokunaga, F, Iwai, K & Kato, K 2012, 'A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex', EMBO Reports, vol. 13, no. 5, pp. 462-468. https://doi.org/10.1038/embor.2012.24
Yagi, Hirokazu ; Ishimoto, Kazuhiro ; Hiromoto, Takeshi ; Fujita, Hiroaki ; Mizushima, Tsunehiro ; Uekusa, Yoshinori ; Yagi-Utsumi, Maho ; Kurimoto, Eiji ; Noda, Masanori ; Uchiyama, Susumu ; Tokunaga, Fuminori ; Iwai, Kazuhiro ; Kato, Koichi. / A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex. In: EMBO Reports. 2012 ; Vol. 13, No. 5. pp. 462-468.
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