MDM2–HDAC1‐mediated deacetylation of p53 is required for its degradation

By A. Ito, Y. Kawaguchi, Chun‐Hsiang Lai, Jeffrey J Kovacs, Y. Higashimoto, E. Appella, T. Yao. EMBO Journal, 2002

605 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/77bc80df3ff4539fd291c69b2588e303fb57f6b4

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In Molecular Biology

1. W. Gu
2. D. Accili
3. Karen H. Vousden
4. J. Kruse
5. C. Brooks
6. Carol Prives
7. E. Masliah
8. Martin F. Lavin

In Oncology

1. W. Gu
2. Karen H. Vousden
3. J. Kruse
4. Carol Prives
5. C. Brooks
6. Martin F. Lavin
7. N. Gueven
8. Vladimir N Uversky

Citations in the corpus

• FoxO1 protects against pancreatic beta cell failure through NeuroD and MafA induction. (2005, background): “Pml targets FoxO1 for ubiquitin-mediated degradation Acetylation affects protein degradation via ubiquitination (Ito et al., 2002; Jeong et al., 2002; Li et al., 2002).”
• Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. (2003, background): “Furthermore, Mdm2 may function in part by recruiting HDAC1 to p53 where it can deacetylate the protein and allow Mdm2 to then ubiquitinate and degrade it [84].”
• The complexity of p53 stabilization and activation (2006, background): “Under unperturbed conditions, MDM2 prevents interaction between p53 and p300.(86) A partner protein of p300, Strap, also increases the level and half-life of p53.”
• Blinded by the Light: The Growing Complexity of p53. (2009, background): “Mdm2 can also recruit the histone deacetylases HDAC1 (Ito et al., 2002) and KAP1 (Wang et al.”
• Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. (2004, background): “However, many HDACs are at least partially cytoplasmic,(10) – 13 and evidence is accumulating that some fraction of these proteins can act on non-histone substrates, including the cytoskeletal protein tubulin and transcription factors such as p53.(10,14,15) Indeed, it has been suggested that regulat”
• p53 ubiquitination: Mdm2 and beyond. (2006, background): “One mechanism that has been shown to occur during times of cellular stress is the direct competition between acetylation and ubiquitination for the same C-terminal lysine residues on p53 (Ito et al., 2002; Li et al., 2002b).”
• Acetylation of tau inhibits its degradation and contributes to tauopathy. (2010, positive): “How might elevated tau acetylation lead to higher levels of p-tau? Acetylation of lysines can preclude its ubiquitination and stabilize proteins that are normally degraded by the UPS, including p53 (Ito et al., 2002), Runx3 (Jin et al.”