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Human MCM4 Protein expressed in Wheat germ - ABIN1310553
Henderson, Hall, Prpic, Hessling, Parker, Sampson, Simkins, Brough, Dixon, Lenz, Knapp, Murphy, Taylor, Fischer, Malinowski: The selection and characterization of antibodies to minichromosome maintenance proteins that highlight cervical dysplasia. in Journal of immunological methods 2011
Data suggest that MCM4 phosphorylation by CDK2 plays role in DNA replication licensing system MCM4/MCM6/MCM7; this phosphorylation interferes with MCM complex function by lowering stability of MCM complex; MCM4 is highly phosphorylated in S phase. (MCM = minichromosome maintenance complex [hexamer of components 4/6/7]; CDK2 = cyclin-dependent kinase-2)
MCM4 and MCM7 expression is significantly correlated with Ki-67, Bmi1, and cyclin E expression in esophageal adenocarcinoma, squamous cell carcinoma and precancerous lesions.
This MCM4 mutation affected human MCM4/6/7 complex formation, since the complex containing the mutant MCM4 protein is unstable and the mutant MCM4 protein is tend to be degraded.
We did not find any evidence of augmented response to a short-term (48 h) cisplatin treatment in these MCM4-deficient cells. However, MCM4-/HPV16+ SiHa cells cannot withstand a prolonged treatment (up to 5 days) of even a sublethal dosage of cisplatin
Purified MCM4/6/7 complex containing the G364R MCM4 exhibited similar levels of single-stranded DNA binding and ATPase activities to the complex containing wild-type MCM4
Mutant p53 depletion profoundly influenced PARP1 localization and increased the level of PCNA and MCM4 proteins.
Of the total, the deregulation of several genes (CDK1, CDK2, CDK4, MCM2, MCM3, MCM4, EIF3a and RPN2) were potentially associated with disease development and progression.
Mcm2-7 loads onto origins during initiation as a double hexamer, yet does not act as a double-stranded DNA pump during elongation.
Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta) protein attenuates vascular lesion formation by inhibition of chromatin loading of minichromosome maintenance complex in smooth muscle cells
point mutation of MCM4 perturbs proper interaction with MCM6 to affect complex formation of MCM4/6/7 that is a core structure of MCM2-7 complex
Mutations in MCM4/PRKDC represent a novel cause of DNA breakage and NK cell deficiency.
Widdrol breaks DNA directly in HT29 cells, resulting in checkpoint activation via Chk2-p53-Cdc25A-p21-MCM4 pathway and finally cells go to G1-phase cell cycle arrest and apoptosis.
partial MCM4 deficiency results in a genetic syndrome of growth retardation with adrenal insufficiency and selective NK deficiency
MCM4 mutation may have a role in adrenal failure, short stature, and natural killer cell deficiency
higher expression in non-small cell lung cancer
MCM4 did not predict patient survival in this series of cutaneous melanomas.
the ability of cytomegalovirus to delay the accumulation of the mini-chromosome maintenance (MCM) complex proteins, represented by MCM2 and MCM4, and prevent their loading onto chromatin, was compromised in the absence of pUL117
the phosphorylation of MCM4 in the checkpoint control inhibits DNA replication, which includes blockage of DNA fork progression, through inactivation of the MCM complex
HU- or UV irradiation-stimulated phosphorylation of MCM4 at several CDK sites led to inhibition of MCM4 helicase activity, consistent with the notion that the phosphorylation of MCM4 is involved in regulation of DNA synthesis in the checkpoint control.
These results suggest that phosphorylation of MCM4 has several distinct and site-specific roles in the function of MCM during the mammalian cell cycle.
Together, these data support a model in which chromosomal abnormalities in Sdl mice result from the ability of MCM4(D573H) to incorporate into MCM complexes and render them inactive.
role of subunits in DNA helicase acdtivity
Substrate preference and helicase actions of mouse MCM4/6/7 helicase complexes.
MCM4 phosphorylation by Cdc7 kinase facilitates its interaction with Cdc45 on chromatin
Hypomorphic alleles of Mcm4 may increase breast cancer risk.
Loss of one allele of cdc2l genefacilitates carcinogen-induced skin carcinogenesis in vivo.
Mcm4(Chaos3) mutation appears to destabilize the MCM2-7 complex, causing impaired DNA replication and may have a causative role in cancer development.
DNA binding and helicase activities of Mcm4/6/7 are significantly stimulated by Cdt1
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 6 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of this protein by CDC2 kinase reduces the DNA helicase activity and chromatin binding of the MCM complex. This gene is mapped to a region on the chromosome 8 head-to-head next to the PRKDC/DNA-PK, a DNA-activated protein kinase involved in the repair of DNA double-strand breaks. Alternatively spliced transcript variants encoding the same protein have been reported.
DNA replication licensing factor mcm4
, MCM4 minichromosome maintenance deficient 4
, minichromosome maintenance protein 4
, DNA replication licensing factor MCM4
, CDC21 homolog
, homolog of S. pombe cell devision cycle 21
, minichromosome maintenance deficient 4
, mini chromosome maintenance deficient 4 homolog
, minichromosome maintenance deficient 4 homolog