Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells.: Probing interactions of ubiquitylation enzymes in living cells

Abstract : Ubiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitin-conjugating 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 organism.
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Methods in Molecular Biology, Humana Press/Springer Imprint, 2016, Proteostasis, 1449, pp.223-41. 〈10.1007/978-1-4939-3756-1_13〉
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Soumis le : jeudi 29 septembre 2016 - 23:23:51
Dernière modification le : lundi 2 juillet 2018 - 16:26:04

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Ewa Blaszczak, Claude Prigent, Gwenaël Rabut. Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells.: Probing interactions of ubiquitylation enzymes in living cells. Methods in Molecular Biology, Humana Press/Springer Imprint, 2016, Proteostasis, 1449, pp.223-41. 〈10.1007/978-1-4939-3756-1_13〉. 〈inserm-01374191〉

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