Fig. 3: LSD1 interactions with nonhistone proteins (I).
From: LSD1: more than demethylation of histone lysine residues
a p53, the pivotal regulator of multiple processes of cellular life (i.e., cell cycle progression, genomic stability and programmed cell death), when dimethylated at lysine 370, assembles with its cofactor 53BP1 and targets chromatin to activate transcription. If LSD1 removes one methyl group from the same lysine, this interaction is abrogated, and the expression of p53 target genes is inhibited. b pRB, the first identified tumor suppressor protein, with the two serine residues phosphorylated as shown is unable to heterodimerize with the E2F1 transcription factor. Both phosphate groups can be removed by the MYPT1 phosphatase, enabling the protein to interact with E2F1. The activity of MYPT1 is, in turn, dependent on the methylation status of lysine 442, which is under the control of LSD1.
