Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells. - Inserm - Institut national de la santé et de la recherche médicale Access content directly
Journal Articles Methods in Molecular Biology Year : 2016

Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast 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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Origin : Files produced by the author(s)
Origin : Files produced by the author(s)
Origin : Files produced by the author(s)
Origin : Files produced by the author(s)
Origin : Files produced by the author(s)
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Dates and versions

inserm-01374191 , version 1 (29-09-2016)

Identifiers

Cite

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, 2016, Proteostasis, 1449, pp.223-41. ⟨10.1007/978-1-4939-3756-1_13⟩. ⟨inserm-01374191⟩
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