Balancing Mdm2 - a Daxx-HAUSP matter

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 deubiqu...

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Veröffentlicht in:	Nature cell biology 2006-08, Vol.8 (8), p.790-791
1. Verfasser:	Ronai, Ze´ev
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biomedical and Life Sciences Cancer Research Carrier Proteins - genetics Carrier Proteins - metabolism Carrier Proteins - physiology Cell Biology Developmental Biology DNA Damage Endopeptidases - metabolism Genetic aspects Humans Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism Intracellular Signaling Peptides and Proteins - physiology Life Sciences Mice Models, Biological news-and-views Nuclear Proteins - genetics Nuclear Proteins - metabolism Nuclear Proteins - physiology Physiological aspects Post-translational modification Protein Binding Proto-Oncogene Proteins c-mdm2 - genetics Proto-Oncogene Proteins c-mdm2 - metabolism Stem Cells Ubiquitin Ubiquitin - metabolism Ubiquitin Thiolesterase Ubiquitin-Specific Peptidase 7
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Beschreibung
Zusammenfassung:	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.
ISSN:	1465-7392 1476-4679
DOI:	10.1038/ncb0806-790