Regulation of LSD1 histone demethylase activity by its associated factors.

By Yu-Jiang Shi, Caitlin Matson, F. Lan, Shigeki Iwase, T. Baba, Yang Shi. Molecules and Cells, 2005

886 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/65c171bd0ed7c4b49cf983c0601e3516cb4674b8

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In Molecular Biology

1. Yi Zhang
2. Yang Shi
3. J. Whetstine
4. Richard A. Young
5. K. Helin
6. C. D. Allis
7. Aviv Regev
8. E. Li

Citations in the corpus

• Reconstructing and reprogramming the tumor propagating potential of glioblastoma stem-like cells (2014, positive): “RCOR2 resides in a complex with PHF21B and the histone methyltransferase LSD1, both of which were also identified as putative core TF targets (Shi et al., 2005; Yang et al., 2011).”
• Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “Gene location analysis demonstrated that LSD1 and BHC80 binding were interdependent, leading to the suggestion that the binding of BHC80 to demethylated K4 may constitute a targeting system leading to the propagation of K4 demethylation and required for the binding of LSD1 (Lan et al. 2007b).”
• Regulation of histone methylation by demethylimination and demethylation (2007, background): “In support of this hypothesis, the LSD1–Co-REST complex works less efficiently on hyperacetylated nucleosomes 38,44 , and LSD1-mediated demethylation of H3K4 peptides is completely abolished when it also contains acetyl groups on K9, K14 and K18 (REF.”
• LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. (2009, background): “It has also been demonstrated that nucleosomal substrate recognition by LSD1 requires proteins like CoREST (Shi et al., 2005) that possess a histone-tail-presenting module, such as the SANT domain, to bridge LSD1 to the chromatin structure.”
• JmjC-domain-containing proteins and histone demethylation (2006, background): “Full enzymatic activity of LSD1 requires its association with other proteins, such as the CoREST (restin corepressor) complex, indicating that regulatory subunits can have a role in modulating demethylase activit”
• Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases (2007, background): “LSD1 is associated with a transcriptional repressor complex that might be involved in the silencing of tumour-suppressor gene”
• Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. (2006, background): “The LSD1 protein interactions have also been shown to play a key role in either facilitating or inhibiting demethylation of more complex substrates (Lee et al., 2005; Shi et al., 2005).”
• Multivalent engagement of chromatin modifications by linked binding modules (2007, background): “and the H3 Lys demethylase function of LSD1, a model has been presented that is consistent with the noted requirement for DNA binding by CoREST in the processing of nucleosomal substrate”
• Enhancer decommissioning by LSD1 during embryonic stem cell differentiation (2012, background): “To gain further insight into the role of LSD1 in ESC differentiation, we investigated whether LSD1 is associated with previously described complexes, including NuRD, cofactor of REST (CoREST), and the androgen receptor/oestrogen receptor complexe”