That, in mice, CHK2 phosphorylated on S460 (corresponding to S456 in humans) is ubiquitinylated by

That, in mice, CHK2 phosphorylated on S460 (corresponding to S456 in humans) is ubiquitinylated by p53-induced RING-H2 protein (PIRH2) and degraded by proteasomes (Bohgaki et al., 2013). In contrast, CHK2 accumulated Polyester Inhibitors medchemexpress within the non-small cell lung carcinoma cell line NCI-H460 immediately after exposure to IR (Zhang et al., 2006) and its stability immediately after DNA harm| Zannini et al.phosphorylated connected motifs containing basic residues upstream of a serine or threonine (Mendoza et al., 2013), further study is needed to know the biochemical capabilities of CHK2 substrates. Several proteins phosphorylated by CHK2 are also substrates of ATM, which includes BRCA1, BRCA2, KAP-1, and p53 (Banin et al., 1998; Gatei et al., 2000; Wang et al., 2004; White et al., 2006; Matsuoka et al., 2007) suggesting that CHK2 reinforces or redirects ATM function. In spite of the identification of .20 CHK2 substrates so far, a large-scale proteomics evaluation of cellular proteins phosphorylated by this kinase, as has been performed for ATM and ATR (Matsuoka et al., 2007), has not however been reported. Such a study would assistance clarify roles of CHK2 within the DDR and in regular cell physiology. Share this post on: