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 journalArticle

    139 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)1328-30
    Number of pages3
    JournalNature Structural & Molecular Biology
    Volume16
    Issue number12
    DOIs
    Publication statusPublished - Dec 2009

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