p53 is regulated by the lysine demethylase LSD1

By Jing Huang, Roopsha Sengupta, Alexsandra B. Espejo, Min Gyu Lee, Jean A. Dorsey, Mario Richter, Susanne Opravil, R. Shiekhattar, M. Bedford, T. Jenuwein and 1 more. Nature, 2007

801 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/a3109ed98d77a3c4b3028072320af055b615a9ca

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Citations in the corpus

Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: involvement in the proliferation of cancer cells through the E2F/RB pathway (2010, background): “Similarly, LSD1 was first reported to be a H3K4 specific demethylase [1], and later found to demethylate histone H3 lysine 9 and p53 [44,45].”
Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers (2011, background): “LSD1 could prevent the accumulation of the dimethyl groups of p53 by demethylating p53K370Me2 and then inhibit the binding of 53BP1 to p53.(28) Likewise, this might be one of the examples how LSD1 could repress p53-mediated transcriptional upregulation and prevent apoptosis and contribute to human c”
Polyamines: molecules with regulatory functions in plant abiotic stress tolerance (2010, background): “LSD1 acts as a histone demethylase, representing an important regulator of chromatin structure and gene expression (Huang et al. 2007).”
Mechanism and regulation of class switch recombination. (2008, background): “53BP1 is a transcriptional coactivator for p53, binding through its tandem Tudor domains to p53 dimethylated at lysine 370 (154).”
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “Methylation-mediated recruitment of 53BP1 may extend to non-histone proteins as well, as a recent report shows that 53BP1 can also bind dimethylated K370 of the tumor suppressor p53 (p53K370me2”
Blinded by the Light: The Growing Complexity of p53. (2009, background): “The demethylase LSD1 removes K370 dimethylation and in doing so prevents p53 from interacting with p53-binding protein 1 (53BP1), a coactivator of p53 (Huang et al., 2007).”
LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. (2009, background): “, 2001), and it has also been shown to interact with p53, repress p53-mediated transcription and inhibit p53-promoted apoptosis (Huang et al., 2007).”
Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “For example, LSD1 not only targets its canonical substrate, histone H3, but also demethylates the tumour suppressor p53 at lysine 370 and represses p53 activitie”
SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells (2015, background): “It was also reported that LSD1 demethylates lysine residues at non-histone proteins including p53, MYPT1, DNMT1 and E2F1 [7-10].”