Abstract
SUMOylation is a widely used protein posttranslational mechanism capable of regulating substrates localization, stability, and/or activity. Identification and characterization of bona fide SUMO substrates is a laborious task but its discovery can shed light to exquisite and crucial regulatory signaling events occurring within the cell. Experiments performed in the SUMOylation field often demand a good understanding of the putative substrate’s function and necessitate a solid knowledge regarding both in vitro and in vivo approaches. This contribution offers a simplified view into some of the most common experiments performed in biochemical and cell biological research of the SUMO pathway in mammalian systems. It also summarizes and updates well established protocols and tricks in order to improve the likelihood to obtain reliable and reproducible results.
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Acknowledgements
Research performed at the laboratory of Pathophysiological Cell Signaling is funded by the following bodies: FWO (G0C7514N grant), BELSPO (IAP-VII/07 program), VUB Research Council (new PI grant), and Innoviris (Brains Back to Brussels program to GJG). CC thanks financial support from the European Union’s Seventh Framework Program (FP7) 2007–2013 under grant agreement no. 264257. The authors would also like to acknowledge networking support by the Proteostasis COST Action (BM1307).
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Cedeño, C., La Monaca, E., Esposito, M., Gutierrez, G.J. (2016). Detection and Analysis of SUMOylation Substrates In Vitro and In Vivo. In: Matthiesen, R. (eds) Proteostasis. Methods in Molecular Biology, vol 1449. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3756-1_16
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DOI: https://doi.org/10.1007/978-1-4939-3756-1_16
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