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Exploring the Rampant Expansion of Ubiquitin Proteomics

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The Ubiquitin Proteasome System

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1844))

Abstract

The ubiquitin proteasome system can arguably affect all cellular proteins with few exceptions. In addition to regulating many pathways such as cell cycle progression, inflammation, gene expression, DNA repair, and vesicle trafficking—to just name a few—ubiquitination can occur to any nascent or newly translated protein that misfolds. In the past years, substantial progress has been achieved in advancing our global understanding of the ubiquitinome—the ensemble of ubiquitinated proteins within a cell—using mass spectrometry-based proteomics. Notably, over 50,000 conjugation sites have now been reported. In this review, we discuss recent proteomics methods used to expand our knowledge of the ubiquitin proteasome system through the identification of ubiquitination sites, poly-ubiquitin chain types, and E3 ubiquitin ligase substrates.

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Acknowledgments

The authors would like to thank all lab members for the discussions and Cristen Molzahn for the comments on the manuscript. They also acknowledge support from the Canadian Institutes of Health Research (CIHR) and British Columbia Proteomics Network (BCPN); TM is a MSFHR new investigator.

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  1. Department of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada

    Amalia Rose & Thibault Mayor

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  1. Amalia Rose
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Correspondence to Thibault Mayor .

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  1. Department of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada

    Thibault Mayor

  2. Department of Chemistry and Biochemistry, University of Nevada Las Vegas, Las Vegas, NV, USA

    Gary Kleiger

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Rose, A., Mayor, T. (2018). Exploring the Rampant Expansion of Ubiquitin Proteomics. In: Mayor, T., Kleiger, G. (eds) The Ubiquitin Proteasome System. Methods in Molecular Biology, vol 1844. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8706-1_22

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