Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne

Tycho E. T. Mevissen, Yogesh Kulathu, Monique P.C. Mulder, Paul P. Geurink, Sarah L. Maslen, Malte Gersch, Paul R. Elliott, John E. Burke, Bianca D. M. van Tol, Masato Akutsu, Farid El Oualid, Masato Kawasaki, Stefan M.V. Freund, Huib Ovaa and David Komander ()
Additional contact information
Tycho E. T. Mevissen: Medical Research Council Laboratory of Molecular Biology
Yogesh Kulathu: Medical Research Council Laboratory of Molecular Biology
Monique P.C. Mulder: Netherlands Cancer Institute, Plesmanlaan 121
Paul P. Geurink: Netherlands Cancer Institute, Plesmanlaan 121
Sarah L. Maslen: Medical Research Council Laboratory of Molecular Biology
Malte Gersch: Medical Research Council Laboratory of Molecular Biology
Paul R. Elliott: Medical Research Council Laboratory of Molecular Biology
John E. Burke: Medical Research Council Laboratory of Molecular Biology
Bianca D. M. van Tol: Netherlands Cancer Institute, Plesmanlaan 121
Masato Akutsu: Medical Research Council Laboratory of Molecular Biology
Farid El Oualid: Netherlands Cancer Institute, Plesmanlaan 121
Masato Kawasaki: Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Stefan M.V. Freund: Medical Research Council Laboratory of Molecular Biology
Huib Ovaa: Netherlands Cancer Institute, Plesmanlaan 121
David Komander: Medical Research Council Laboratory of Molecular Biology

Nature, 2016, vol. 538, issue 7625, 402-405

Abstract: The structures of the deubiquitinating enzyme Cezanne alone or in complex with its substrate or product are solved, showing how Cezanne specifically targets Lys11-linked polyubiquitin.

Date: 2016
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DOI: 10.1038/nature19836

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