Title : Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.

Pub. Date : 2016 Jun 2

PMID : 27210019






5 Functional Relationships(s)
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1 Lysines in the tetramerization domain of p53 selectively modulate G1 arrest. Lysine tumor protein p53 Homo sapiens
2 By changing lysines 351 and 357 to arginine, thereby blocking all post-translational modifications of these residues, DNA binding and transcriptional regulation by p53 remain virtually unchanged. Lysine tumor protein p53 Homo sapiens
3 On the other hand, by changing these lysines to glutamine (2KQ-p53), thereby neutralizing their positive charge and potentially mimicking acetylation, p53 is impaired in the induction of cell cycle arrest and yet can still effectively induce cell death. Lysine tumor protein p53 Homo sapiens
4 On the other hand, by changing these lysines to glutamine (2KQ-p53), thereby neutralizing their positive charge and potentially mimicking acetylation, p53 is impaired in the induction of cell cycle arrest and yet can still effectively induce cell death. Lysine tumor protein p53 Homo sapiens
5 Our findings show that strong induction of p21 is not sufficient to block H1299 cells in G1, and imply that modification of one or both of the lysines within the tetramerization domain may serve as a mechanism to shunt p53 from inducing cell cycle arrest. Lysine tumor protein p53 Homo sapiens