In this study we demonstrated for the first time that MCM2 among MCM2-7 except for MCM5 is specifically degraded and that MCM2 and MCM7 are localized in the cytoplasm in senescent cells. To examine the relationship between the cytoplasmic localization of MCM proteins and cell cycle phase the distribution of DNA content of cells showing cytoplasmic localization of MCM2 and MCM7 was examined.
Our study confirms that MCM7 is a valuable marker for assessing the progression of pancreatic neuroendocrine tumors especially in patients with early stage disease and without distant metastasis.
Here the authors show that in human cells cohesin loading onto chromosomes during early S phase requires the replicative helicase MCM2-7 and the kinase DDK. Cohesin and its loader SCC2/4 (NIPBL/MAU2 in humans) associate with DDK and phosphorylated MCM2-7.
CDT1 MCM7 and NUDT1 were shown to be up-regulated in hepatocellular carcinoma tissues and provide a more accurate diagnosis than alpha-fetal protein alone.
Data suggest that interaction of Mcm10 with Mcm2-7 multimer requires Mcm10 domain that contains amino acids 530-655 which overlaps with domain required for stable retention of Mcm10 on chromatin; Mcm10 conserved domain (amino acids 200-482) is essential for DNA replication; both conserved domain and Mcm2-7-binding domain are required for full activity of Mcm10.
Our results indicate that MCM7 may exert certain functions on spindle formation to prevent cytokinesis during early mitosis by regulating CDK1 activity.
MCM7 is helpful for us to make differential diagnosis in pathological grade MCM7 combination of Ki67 may serve as more sensitive proliferation markers for evaluation of gastric carcinoma and precancerous lesions
Data indicate that RACK1 increases interactions between Akt and MCM7 and promotes Akt-dependent MCM7 phosphorylation which in turn increases MCM7 binding to chromatin and miniature chromosome maintenance (MCM) complex formation.
The results clearly demonstrate 7q21-22 amplification MCM7 and its intronic miR-25 are the major molecular switches involved in the complex oncogenic circuits of gastric cancer.
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