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

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

doi:10.1038/nsmb.1731

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 journal › Article › peer-review

171 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 language	English
Pages (from-to)	1328-30
Number of pages	3
Journal	Nature Structural & Molecular Biology
Volume	16
Issue number	12
DOIs	https://doi.org/10.1038/nsmb.1731
Publication status	Published - Dec 2009

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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.",

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AU - Hofmann, Kay

AU - Komander, David

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

Abstract

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