Direct activation of protein kinases by unanchored polyubiquitin chains

Zong-Ping Xia, Lijun Sun, Xiang Chen, Gabriel Pineda, Xiaomo Jiang, Anirban Adhikari, Wenwen Zeng and Zhijian J. Chen ()
Additional contact information
Zong-Ping Xia: Department of Molecular Biology,
Lijun Sun: Department of Molecular Biology,
Xiang Chen: Department of Molecular Biology,
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,

Nature, 2009, vol. 461, issue 7260, 114-119

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.

Date: 2009
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DOI: 10.1038/nature08247

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