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Ubiquitin-like protein activation

Oncogene volume 23, pages 1958–1971 (2004)Cite this article

Abstract

Post-translational covalent attachment of ubiquitin and ubiquitin-like proteins (ubls) has emerged as a predominant cellular regulatory mechanism, with important roles in controlling cell division, signal transduction, embryonic development, endocytic trafficking and the immune response. Ubls function by remodeling the surface of their target proteins, changing their target's half-life, enzymatic activity, protein–protein interactions, subcellular localization or other properties. At least 10 different ubiquitin-like modifications exist in mammals, and attachment of different ubls to a target leads to different biological consequences. Ubl-conjugation cascades are initiated by activating enzymes, which also coordinate the ubls with their downstream pathways. A number of biochemical and structural studies have provided insights into the mechanism of ubl-activating enzymes and their roles in ubl conjugation cascades.

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Acknowledgements

We are grateful to Art Haas for helpful discussions and communication of results prior to publication. This work was supported by ALSAC, the NIH (P30CA21765 NCI Cancer Center Core grant to St. Jude, R01GM69530 to BAS) and a Pew Scholar Award in Biomedical Sciences to BAS.

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  1. Department of Structural Biology, St Jude Children's Research Hospital, Memphis, 38105, TN, USA

    Danny T Huang, Helen Walden, David Duda & Brenda A Schulman

  2. Department of Genetics, Tumor Cell Biology, St Jude Children's Research Hospital, Memphis, 38105, TN, USA

    Danny T Huang, Helen Walden, David Duda & Brenda A Schulman

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Huang, D., Walden, H., Duda, D. et al. Ubiquitin-like protein activation. Oncogene 23, 1958–1971 (2004). https://doi.org/10.1038/sj.onc.1207393

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