Recent advances in defining the ubiquitylome
- Creators
- Porras-Yakushi, Tanya R.
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Hess, Sonja
Abstract
Ubiquitin is a small 8.5 kDa protein that is conjugated to a target protein in a concerted three step enzymatic process. Ubiquitin addition can drastically affect function or target the modified protein for degradation. Ubiquitin modifications have important regulatory roles in disease progression, such as in cancer and neurodegenerative diseases to name a few. As a consequence, it is imperative to identify important ubiquitin targets to elucidate the role of the modification. Proteomic studies have sought to understand this role by identifying proteome-wide ubiquitylated proteins. Two central ideas have developed to characterize the ubiquitylome: affinity purification of ubiquitylated proteins and optimization of GG-peptide enrichment. In this review, we will discuss recent advances in both approaches and discuss how these studies are essential to pharmacoproteomics.
Additional Information
© 2014 Informa UK Ltd. We acknowledge all of the scientific contributions made by all the other researchers in the field who were not cited in this review. We apologize for not including your work, however, due to space constraints we were unable to include more of the amazing work being performed in the field of ubiquitylation and mass spectrometry-based proteomics. We thank Raymond J Deshaies for his insight and lively discussions. Lastly, we thank the members of the Sonja Hess Laboratory in the Proteome Exploration Laboratory for their lively discussions and helpful suggestions. Financial & competing interests disclosure: The Proteome Exploration Laboratory is supported by the Beckman Institute, the Gordon and Betty Moore Foundation through Grant GBMF775 and the NIH through grants SRR029594A and 1S10OD010788. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed. No writing assistance was utilized in the production of this manuscript.Additional details
- Eprint ID
- 47365
- DOI
- 10.1586/14789450.2014.926223
- Resolver ID
- CaltechAUTHORS:20140721-104442625
- Caltech Beckman Institute
- GBMF775
- Gordon and Betty Moore Foundation
- SRR029594A
- NIH
- 1S10OD010788
- NIH
- Created
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2014-07-21Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field