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Direct activation of protein kinases by unanchored polyubiquitin chains

Author

Listed:
  • Zong-Ping Xia

    (Department of Molecular Biology,)

  • Lijun Sun

    (Department of Molecular Biology,
    Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, Texas 75390-9148, USA)

  • Xiang Chen

    (Department of Molecular Biology,
    Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, Texas 75390-9148, USA)

  • Gabriel Pineda

    (Department of Molecular Biology,)

  • Xiaomo Jiang

    (Department of Molecular Biology,)

  • Anirban Adhikari

    (Department of Molecular Biology,)

  • Wenwen Zeng

    (Department of Molecular Biology,)

  • Zhijian J. Chen

    (Department of Molecular Biology,
    Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, Texas 75390-9148, USA)

Abstract

Unanchored polyubiquitin chains The nuclear factor κ enhancer binding protein (NF-κB) signalling pathway is important for a range of cellular processes including immune function. Here Xia et al. show that free Lys63 polyubiquitin chains generated, which are not linked to any protein substrates, can directly activate kinases in the NK- κB signalling pathway. Disassembly of the polyubiquitin chains by deubiquitination enzymes prevented kinase activation. These results suggest that unanchored polyubiquitin chains much like second messengers can directly activate kinases in immune and inflammatory pathways.

Suggested Citation

  • Zong-Ping Xia & Lijun Sun & Xiang Chen & Gabriel Pineda & Xiaomo Jiang & Anirban Adhikari & Wenwen Zeng & Zhijian J. Chen, 2009. "Direct activation of protein kinases by unanchored polyubiquitin chains," Nature, Nature, vol. 461(7260), pages 114-119, September.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7260:d:10.1038_nature08247
    DOI: 10.1038/nature08247
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