IndraLab
Statements
sparser
"In order to improve our understanding of the Smyd2 catalytic cycle, here we carried out μ‐second MD simulations of the following systems (see Fig. xref ): Smyd2 in complex with AdoMet cofactor (Model‐A); Smyd2‐AdoMet‐p53 peptide (unmethylated) complex (Model‐B); Smyd2‐AdoHcy‐p53 peptide (methylated at Lys370) complex (Model‐C); and Smyd2‐AdoMet in complex with the p53 peptide methylated at Lys372 (Model‐D)."
sparser
"We and others have reported that aberrant methylation of oncoproteins and tumor suppressor proteins plays important roles in development/progression processes of a variety of human cancers. xref , xref Our previous studies indicated that methylation on non‐histone proteins affected subcellular localization, stability, and other modifications of several oncogenic proteins; xref , xref , xref , xref for example, methylation of heat shock protein 70 by SETD1A promotes its nuclear translocation and interaction with Aurora kinase B. xref We have also shown that demethylation of lysine residues in MYPT1, a retinoblastoma 1 phosphorylation regulator, by lysine‐specific histone demethylase 1 destabilizes the MYPT1 protein and promotes cell cycle progression in cancer cells. xref Other groups showed that methylation of lysine 372 of p53 by SETD7 increases protein stability and enhances p53 activity, xref whereas monomethylation of lysine 370 by SMYD2 represses p53 function. xref Furthermore, the activities of several protein kinases were shown to be under the control of lysine methylation; methylation of vascular endothelial growth factor receptor 1 xref and AKT1 xref by SMYD3 leads to enhancement of autophosphorylation."