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The JAMM in the proteasome

Nature Structural & Molecular Biology volume 21, pages 346–348 (2014)Cite this article

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Structures of the deubiquitinating enzyme Rpn11 of the proteasomal 19S regulatory particle reveal its role in hydrolyzing the proximal ubiquitin from a protein that is about to be degraded.

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Figure 1: Refined role of Rpn11 in the proteasome.

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Acknowledgements

We would like to thank P. da Fonseca for comments on the manuscript. Work in the authors' laboratory is supported by the UK Medical Research Council (U105192732), the European Research Council (309756) and the Lister Institute for Preventive Medicine.

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Authors and Affiliations

  1. Tobias Wauer and David Komander are at the Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.,

    Tobias Wauer & David Komander

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  1. Tobias Wauer
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  2. David Komander
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Correspondence to David Komander.

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Competing interests

DK is a part of the DUB Alliance that includes Cancer Research Technology and FORMA Therapeutics.

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Wauer, T., Komander, D. The JAMM in the proteasome. Nat Struct Mol Biol 21, 346–348 (2014). https://doi.org/10.1038/nsmb.2800

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