The ubiquitin ligase COP1 is a critical negative regulator of p53

By D. Dornan, I. Wertz, Harumi Shimizu, D. Arnott, G. Frantz, P. Dowd, Karen O' Rourke, H. Koeppen, V. Dixit. Nature, 2004

784 citations recorded by the source corpus.

Subfields: Biotechnology, Cancer Research, Oncology

View Paper: https://www.semanticscholar.org/paper/6ce01c4e8ad597f900f13ffc38a676bbe698d878

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In Biotechnology

1. W. Gu
2. Arnold J. Levine

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1. W. Gu
2. C. Brooks

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Citations in the corpus

• IAPs, RINGs and ubiquitylation (2005, background): “And, as if this were not complicated enough, two recently described p53 E3 ligases, COP1 (Ref”
• Acetylation is indispensable for p53 activation. (2008, background): “To extend these findings, we identified Pirh2 as another p53 target (Leng et al., 2003), whose induction by p53 is independent of the acetylation status (Figure S10).”
• The regulation of AMPK beta1, TSC2, and PTEN expression by p53: stress, cell and tissue specificity, and the role of these gene products in modulating the IGF-1-AKT-mTOR pathways. (2007, background): “identified p53-targeted genes that have p53-ubiqutin ligase activity (41, 42).”
• Role of p53 in Cell Death and Human Cancers (2011, background): “In addition to MDM2, RING-finger type E3 ubiquitin protein ligases Pirh2 (p53-induced RING H2 domain protein) [59] and COP1 (constitutive photomorphogenic 1) [60,61] also interact with p53 and mediate the ubiquitin/proteasome-dependent degradation of p53 in an MDM2-independent manner.”
• The p53 pathway: positive and negative feedback loops (2005, background): “Surprisingly, there appears to be three different p53-ubiqutin ligase activities (MDM-2, Cop-1 and Pirh-1), each of which forms an autoregulatory loop resulting in lower p53 activity (Leng et al., 2003; Dornan et al., 2004) (Figure 10).”
• The ConsensusPathDB interaction database: 2013 update (2012, background): “The module also includes gene sets centered at several ubiquitin E3 ligases: COP1 [gene symbol: RFWD2, a negative regulator of p53 (39)], RBX1 (Gene Ontology annotation: DNA repair) and DDB2 complex [involved in DNA repair (40)].”
• ROS and p53: a versatile partnership. (2008, background): “In unstressed mammalian cells, p53 has a short half-life and is normally maintained at low levels by continuous ubiquitylation catalyzed by Mdm2 [22], COP1 (constitutively photomorphogenic 1) [23], and Pirh2 (p53-induced protein with a RING-H2 domain) [24], and subsequent degradation by 26S proteaso”
• p53 ubiquitination: Mdm2 and beyond. (2006, background): “Another E3 ligase, COP1, has also been described recently as a direct ubiquitin ligase for p53 (Dornan et al., 2004).”
• Driver mutations in TP53 are ubiquitous in high grade serous carcinoma of the ovary (2010, background): “Of the remaining mutation-negative cases, three may have had inactivation of the p53 pathway through chromosomal gain at the MDM2 or MDM4 loci or potentially other genes that alter p53 function in trans such as RFWD2 and RCHY1 [25,26].”
• The Ubiquitin-Proteasome Pathway and Plant Development (2004, background): “It will be interesting to learn the full extent of COP1’s influence on growth and development.”
• A QTL for rice grain width and weight encodes a previously unknown RING-type E3 ubiquitin ligase (2007, background): “Many RING-type proteins function as E3 ubiquitin-protein ligases, targeting proteins for ubiquitin-dependent degradation by the 26S proteasom”