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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 publication

DOI

10.1007/978-1-4939-6439-0_10

Type

Journal article

Journal

Methods in molecular biology (Clifton, N.J.)

Publication Date

01/2017

Volume

1491

Pages

131 - 144

Addresses

Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, UK. benedikt.kessler@ndm.ox.ac.uk.

Keywords

Humans, DNA Repair, Mass Spectrometry, Sumoylation