Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain

Yogesh Kulathu, Masato Akutsu, Anja Bremm, Kay Hofmann, David Komander

Research output: Contribution to journalArticlepeer-review

143 Citations (Scopus)

Abstract

The protein kinase TAK1 is activated by binding to Lys63 (K63)-linked ubiquitin chains through its subunit TAB2. Here we analyze crystal structures of the TAB2 NZF domain bound to Lys63-linked di-and triubiquitin, revealing that TAB2 binds adjacent ubiquitin moieties via two distinct binding sites. The conformational constraints imposed by TAB2 on a Lys63 dimer cannot be adopted by linear chains, explaining why TAK1 cannot be activated by linear ubiquitination events.

Original languageEnglish
Pages (from-to)1328-1330
Number of pages3
JournalNature Structural and Molecular Biology
Volume16
Issue number12
DOIs
Publication statusPublished - 2009 Dec
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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