A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus

By L. Mayo, D. Donner. Proceedings of the National Academy of Sciences of the United States of America, 2001

1,287 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/3144ffd9bfd3b24a9b1fdde79f0e297d2f9dbffb

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In Cancer Research

1. B. Kaina
2. F. McCormick
3. Xin Lu
4. Carlos L. Arteaga
5. Karen H. Vousden
6. A. Bader
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In Molecular Biology

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In Oncology

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5. Arkaitz Carracedo
6. Xin Lu
7. B. Kaina
8. W. Roos

Citations in the corpus

• Oncogenic PI3K deregulates transcription and translation (2005, background): “77 ), and also suppresses p53 activity by a mechanism that involves MDM2 (murine double minute”
• PI3K/Akt and apoptosis: size matters (2003, background): “Two alternative mechanisms of Aktdependent regulation of Mdm2/HDM2 have been described, and they include the induction of Mdm2 nuclear import (Mayo and Donner, 2001) or the regulation of Mdm2/HDM2-ubiquitin ligase enzymatic activity (Zhou et al., 2001b; Ashcroft et al., 2002; Ogawara et al., 2002).”
• DNA damage-induced cell death: from specific DNA lesions to the DNA damage response and apoptosis. (2013, background): “It binds to and phosphorylates Mdm2, the ubiquitin E3 ligase, on Ser166 and Ser186 thereby inducing its nuclear import or increasing its ubiquitin ligase activity [173,174].”
• The PTEN–PI3K pathway: of feedbacks and cross-talks (2008, background): “…proteins, such as BAD, MDM2 and members of the Forkhead family (del Peso et al., 1997; Biggs et al., 1999; Brunet et al., 1999; Guo et al., 1999; Kops et al., 1999; Nakae et al., 1999; Rena et al., 1999; Takaishi et al., 1999; Tang et al., 1999; Mayo and Donner, 2001; Ashcroft et al., 2002).”
• PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. (2007, background): “Phosphorylation of HDM2 by Akt causes the ligase to translocate from the cytosol to the nucleus where it binds and inhibits the function of p53, subsequently promoting its translocation to the cytosol and subsequent ubiquitin-mediated degradation (Mayo and Donner, 2001).”