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Publisher
Humana Press, New York, NY
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Authors: Ewa Blaszczak Claude Prigent Gwenaël Rabut
Publish Date: 2016
Volume: , Issue: , Pages: 223-241
Abstract
Ubiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitinconjugating enzymes E2s and ubiquitin ligases E3s These enzymes form transient complexes with each other and their modification substrates and determine the nature of the ubiquitin signals attached to their substrates One challenge in the field of protein ubiquitylation is thus to identify the E2–E3 pairs that function in the cell In this chapter we describe the use of bimolecular fluorescence complementation to assay E2–E3 interactions in living cells using budding yeast as a model organismThis work received funding from the ANR grant ANR12JSV80003001 and Biosit GR was supported by INSERM and EB received fellowships from the Ministère de la Recherche et de l’Enseignement Supérieur and La Ligue Contre le Cancer Confocal microscopy was performed at the Microscopy Rennes Imaging Center MRic facility The authors also would like to acknowledge networking support by the Proteostasis COST Action BM1307
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