Biochemical and Mass Spectrometry-Based Approaches to Profile SUMOylation in Human Cells

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Benedikt M Kessler, Sara Bursomanno, Joanna F McGouran, Ian D Hickson, Ying Liu

Posttranslational modification of proteins with the small ubiquitin-like modifier (SUMO) regulates protein function in the context of cell cycle and DNA repair. The occurrence of SUMOylation is less frequent as compared to protein modification with ubiquitin, and appears to be controlled by a smaller pool of conjugating and deconjugating enzymes. Mass spectrometry has been instrumental in defining specific as well as proteome-wide views of SUMO-dependent biological processes, and several methodological approaches have been developed in the recent past. Here, we provide an overview of the latest experimental approaches to the study of SUMOylation, and also describe hands-on protocols using a combination of biochemistry and mass spectrometry-based technologies to profile proteins that are SUMOylated in human cells.

Original languageEnglish
Title of host publicationActivity-Based Proteomics : Methods and Protocols
EditorsHerman S. Overkleeft, Bogdan I. Florea
Number of pages14
Volume1491
PublisherHumana Press
Publication date2017
Pages131-144
Chapter10
ISBN (Print)978-1-4939-6437-6
ISBN (Electronic)978-1-4939-6439-0
DOIs
Publication statusPublished - 2017
SeriesMethods in Molecular Biology
Volume1491
ISSN1064-3745

ID: 169993150