Regulation of p53 activity through lysine methylation

By S. Chuikov, Julia K. Kurash, Jon R. Wilson, B. Xiao, N. Justin, G. Ivanov, K. Mckinney, Paul Tempst, Carol Prives, S. Gamblin and 2 more. Nature, 2004

845 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/fb8f264373c6bd23ac28e59b458e9b59d308e5ec

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

In Oncology

Citations in the corpus

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. (2006, methodology): “RNAi for SirT2 was generated and performed as described using a lentiviral system (Chuikov et al. 2004), in conjunction with the sequence 5 -GACTCCAAGAAGGCCTACA-3 .”
Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. (2006, background): “K120 Acetylation Is Catalyzed by Tip60, but Not CBP/p300 or PCAF K120 is located in the L1 loop of the DNA-binding core domain of p53 ( Cho et al., 1994; Huyen et al., 2004).”
p53 ubiquitination: Mdm2 and beyond. (2006, background): “…that occur on p53 and Mdm2 during times of cell stress (Brooks and Gu, 2003), although additional modifications have also been identified under certain conditions, including sumoylation, neddylation, and methylation (Chuikov et al., 2004; Rodriguez et al., 1999; Xirodimas et al., 2004).”
Blinded by the Light: The Growing Complexity of p53. (2009, background): “Methylation of K372 by the SET domain methyltransferase Set9 leads to increased p21 expression (Chuikov et al., 2004), but whether this has a selective impact on p53 target gene activation has not been determined.”
The SET-domain protein superfamily: protein lysine methyltransferases (2005, background): “to methylate p53, increasing the stability of this short lived tumor-suppressor protein [38].”
The complexity of p53 stabilization and activation (2006, background): “Another modification in the same region of the molecule, methylation, also regulates the activity of p53.(89) Overexpression of the Set9 methyltransferase caused hyperstabilization and activation of nuclear p53 and increased apoptosis.”
The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. (2007, background): “Importantly, among histone methyltransferases, SET7/9 and SMYD2 have been shown to methylate nonhistone proteins (9, 10 , 19).”
Methylation multiplicity and its clinical values in cancer (2021, positive): “P53 mono-and di-methylation at Lys 370 by SMYD2 repress and enhance its transcription, respectively (Refs 78 – 80), and both mono-and di-methylation of Lys 370 are inhibited by the di-methylation of the neighbouring Lys 372 by SETD7 (Ref.”
Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “Recent studies revealed that Lys370, Lys372, and Lys382 can also be methylated (Chuikov et al., 2004; Huang et al., 2006b; Shi et al., 2007), indicating that acetylation would prevent methylation.”
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, background): “The interactions of p53 and 14-3-3 with their partners as reported previously [61,64-79] are examined herein but from an order-disorder point of view.”
Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B (2012, neutral): “IB: HA (AURKB) HA–AURKB – – + – + – FLAG–AURKB-[1-200] FLAG–AURKB-[201-344]”