Review Article | Published:

Constructing and decoding unconventional ubiquitin chains

Nature Structural & Molecular Biology volume 18, pages 520528 (2011) | Download Citation

Abstract

One of the most notable discoveries in the ubiquitin system during the past decade is the extensive use of diverse chain linkages to control signaling networks. Although the utility of Lys48- and Lys63-linked chains in protein turnover and molecular assembly, respectively, are well known, we are only beginning to understand how unconventional chain linkages are formed on target proteins and how such linkages are decoded by specific binding proteins. In this review, we summarize recent efforts to elucidate the machinery and mechanisms controlling assembly of Lys11-linked and linear (or Met1-linked) ubiquitin chains, and describe current models for how these chain types function in immune signaling and cell-cycle control.

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Acknowledgements

We would like to thank M. Rape (University of California, Berkeley) and D. Komander (Medical Research Council) for providing coordinates for the structural models of ubiquitin and UBE2S. J.W.H. is supported by the US National Institutes of Health and Millennium Pharmaceuticals. C.B. is supported by the Emmy Noether Programm of the Deutsche Forschungsgemeinschaft.

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Affiliations

  1. Institute of Biochemistry II, Goethe University School of Medicine, Frankfurt, Germany.

    • Christian Behrends
  2. Departments of Pathology and Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.

    • J Wade Harper

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Competing interests

J.W.H. is a consultant for Millennium Pharmaceuticals.

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Correspondence to J Wade Harper.

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DOI

https://doi.org/10.1038/nsmb.2066

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