Mansfeld (Guestgroup)
The coordination of proliferation with quiescence and differentiation is fundamental for multicellular life and development. The decision on whether cells keep dividing, or whether they temporally or permanently exit from the cell cycle is tightly controlled by ubiquitin-mediated proteolysis. Ubiquitin-mediated proteolysis requires the sequential interplay of three enzymes E1, E2, and ubiquitin E3 ligases. E3 ligases recognise and covalently modify crucial substrates such cell cycle regulators with chains of ubiquitin molecules and thereby target them for degradation by the 26S proteasome. Emerging evidence indicates that mutations in components of the ubiquitin proteasome system are a hallmark of multiple cancers and in addition interfere with faithful development and differentiation.
Our lab combines cell biological and biochemical approaches to reveal how the ubiquitin system controls cell cycle progression and the exit into quiescence and differentiation using human cells a model. For more information on our research please visit our lab page.
Contact at BIOTEC:
Assistant to Group Leader
NameGloria Marchesi
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Visitor Address:
Biotechnologisches Zentrum Tatzberg 47/49
01307 Dresden