New Insights into p53 Signaling and Cancer Cell Response to DNA Damage: Implications for Cancer Therapy

Figure 1

Structure and posttranscriptional modification of the human p53 protein. Circles, Ser/Thr phosphorylation sites; squares, acetylation sites; hexagon, SUMOylation site. The insert vertical bars above the DNA-binding domain illustrate the distribution and the prevalence of point mutations found in p53 in human cancers [19, 20]. The most frequently mutated codons (“hotspot” codons) are identified. Several proteins that phosphorylate p53 and the target amino acids of p53 are also shown in the box [21]. ATM, ataxia-telangiectasia mutated; ATR, ataxia-telangiectasia and RAD3 related; DNA-PK, DNA-dependent protein kinase; mTOR; mammalian target of rapamycin; CHK1 and 2, checkpoint kinases 1 and 2; p38k, p38 kinase; GSK3β, glycogen synthase kinase-3 beta; HIPK2, homeodomain interacting protein kinase 2; JNK, c-Jun-NH(2)-terminal kinase; PKC, protein kinase C; CK2, casein kinase 2; PKR, protein kinase R.