NDLI: The ubiquitin–protein ligase Itch regulates p73 stability

Content Provider	PubMed Central
Author	Rossi, Mario Laurenzi, Vincenzo De Munarriz, Eliana Green, Douglas R. Liu, Yun-cai Vousden, Karen H. Gianni, Cesareni Melino, Gerry
Copyright Year	2005
Abstract	p73, a member of the p53 family of transcription factors, is upregulated in response to DNA damage, inducing cell cycle arrest and apoptosis. Besides indications that this p73 response is post-transcriptional, little is known about the underlying molecular mechanisms of p73 protein degradation. Ubiquitination and proteasomal-dependent degradation of p53 are regulated by its transcriptional target MDM2. However, unlike p53, p73 binds to, but is not degraded by, MDM2. Here we describe the binding of p73 to Itch, a Hect ubiquitin–protein ligase. Itch selectively binds and ubiquitinates p73 but not p53; this results in the rapid proteasome-dependent degradation of p73. Upon DNA damage Itch itself is downregulated, allowing p73 protein levels to rise and thus interfere with p73 function. In conclusion, we have identified a key mechanism in the control of p73 protein levels both in normal as well as in stress conditions.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7600444
Starting Page	836
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	4
Volume Number	24
Language	English
Publisher Date	2005-02-23
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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The ubiquitin–protein ligase Itch regulates p73 stability