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Balancing Mdm2 — a Daxx–HAUSP matter

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RING-finger ubiquitin ligases elicit ubiquitination of their substrates, which is balanced by their self-ubiquitination. New insights into regulating the switch between these two modes are illustrated by the role of the adaptor protein Daxx (death domain-associated protein) in regulating the deubiquitinating enzyme HAUSP which, in turn, directs the ligase activity of Mdm2.

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Figure 1: Under non-stress conditions, Daxx associates with HAUSP and Mdm2, which results in stabilization of Mdm2 and MdmX and direction of Mdm2 ligase activity toward p53 that, in turn, leads to p53 ubiquitination and degradation.

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  1. the Signal Transduction Program, Burnham Institute for Medical Research, La Jolla, CA 92037, USA

    Ze´ev Ronai

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  1. Ze´ev Ronai
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Ronai, Z. Balancing Mdm2 — a Daxx–HAUSP matter. Nat Cell Biol 8, 790–791 (2006). https://doi.org/10.1038/ncb0806-790

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