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Origin and function of ubiquitin-like proteins

Nature volume 458, pages 422–429 (2009)Cite this article

Abstract

Eukaryotic proteins can be modified through attachment to various small molecules and proteins. One such modification is conjugation to ubiquitin and ubiquitin-like proteins (UBLs), which controls an enormous range of physiological processes. Bound UBLs mainly regulate the interactions of proteins with other macromolecules, for example binding to the proteasome or recruitment to chromatin. The various UBL systems use related enzymes to attach specific UBLs to proteins (or other molecules), and most of these attachments are transient. There is increasing evidence suggesting that such UBL–protein modification evolved from prokaryotic sulphurtransferase systems or related enzymes. Moreover, proteins similar to UBL-conjugating enzymes and UBL-deconjugating enzymes seem to have already been widespread at the time of the last common ancestor of eukaryotes, suggesting that UBL–protein conjugation did not first evolve in eukaryotes.

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Figure 1: Cellular processes that depend on ubiquitin conjugation.
Figure 2: Polyubiquitin-tagged proteins are often targeted for proteasome-mediated degradation.
Figure 3: General functions of UBL tagging.
Figure 4: At the crossroads of UBL–protein modification and sulphur transfer.

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Acknowledgements

I thank V. J. Rubenstein, A. Kusmierczyk and J. Bloom for comments on the manuscript. Work in my laboratory is funded by grants from the National Institutes of Health.

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  1. Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, PO Box 208114, New Haven, Connecticut 06520, USA.,

    Mark Hochstrasser

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Hochstrasser, M. Origin and function of ubiquitin-like proteins. Nature 458, 422–429 (2009). https://doi.org/10.1038/nature07958

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