MCM7

Official Full Name

minichromosome maintenance complex component 7

Organism

Homo sapiens

GeneID

4176

Background

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 the 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, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumorsuppressor protein RB1/RB. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Synonyms

MCM2; CDC47; P85MCM; P1CDC47; PNAS146; PPP1R104; P1.1-MCM3;

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Detailed Information

Minichromosome maintenance proteins 7 (MCM7) are members of the family of minichromosome maintenance proteins (MCMs). MCMs are a class of highly conserved proteins that were first discovered in yeast and subsequently confirmed to be present in eukaryotic cell biology. The MCMs family consists of at least six members: MCM2, MCM3, MCM4, MCM5, MCM6 and MCM7. They have a similar structure and function, participate in the replication and extension of DNA, ensure that DNA is replicated only once per cell cycle, and is closely related to cell proliferation.

The Role of MCM7

The MCM2-7 complex has an extremely important function in DNA replication and is also a focal point for many signaling pathways during cell growth. The MCM4/MCM6/MCM7 complex has ssDNA-dependent ATPase activity, ATP-dependent ssDNA binding activity, and DNA dextran activity. The formation of tumors is caused by various physical and chemical factors, growth factors, proto-oncogenes and other conditions, resulting in uncontrolled cell cycle, abnormal cell differentiation and proliferation. Therefore, MCM7 regulates the cell cycle in G1 and S phases. Cell production, proliferation and tumor formation are closely related.

The ATPase motif of MCM7 is the key to the MCM4 / MCM6 / MCM7 complex. In addition to the common central structure, MCM7 also has a special structure, the zinc finger motif, which exists only in the MCM2 / MCM4 / MCM6 / MCM7 complex and is an essential structure for the regulation of the melting enzyme. Studies have shown that the mRNA level of MCM7 is consistent with the cell cycle, which can be detected significantly in G1 and S phases, but its expression level is gradually decreased or even undetectable in G0 phase and differentiation and senescence. Therefore, MCM7 can be used as a reliable marker for cell proliferation and is one of the basis for diagnosis of tumors.

Figure 1. Roles of MCM phosphorylation mediated by p56Lyn, Akt and ILK in cancer development. （Liangru, et al. 2018）

MCM7 Related Protein

In the cell cycle, CDK can actively phosphorylate MCMs, inactivate the helicase of MCM4 / MCM6 / MCM7, and regulate DNA replication. The regulation of mitotic kinase integrates the MCM2-7 complex into the chromatin; the MCM2-7 complex is treated to be an active helicase at the replication fork by a coordinated action of cdc7/dbf4 and cyclin E/Cdk2 in the G1-S phase transition, initiating DNA replication. Normally, when the cells enter the S phase, the complex is decomposed under the action of high CDK activity to inhibit DNA replication. Thus, in the cell cycle, p16 and MCM7 participate in cell cycle regulation through interaction with CKD, allowing DNA replication and cell proliferation to be performed accurately and orderly.

The receptor for activated C kinase 1 (RACK1) and MCM7 is involved in and regulate the cell cycle. There are multiple phosphorylation sites in the MCM7 and MCMs complex, and phosphorylated MCM7 plays an important role in DNA replication. It was found that RACK1 promotes phosphorylation of the silk/threonine site in MCM7, and phosphorylation of MCM7 promotes cell entry from the G1 phase to the S phase, promoting cell proliferation. A large number of studies have shown that RACK1 is expressed in most tumors, such as breast cancer, ovarian cancer, liver cancer, oral squamous cell carcinoma and malignant melanoma, and promotes tumor formation.

References:

Liangru, F. , & Hongtao, X. . (2018). Role of mcm2–7 protein phosphorylation in human cancer cells. Cell & Bioscience, 8(1), 43-.
Zielecka-Dębska, D. M., Hao, A., Matkowski, R., Kornafel, J., & Szelachowska, J. (2017). Influence of the MCM7 Protein Expression on Oral Cancer Patient Prognosis, Using Different Methods of the Measurement. International Journal of Radiation Oncology• Biology• Physics, 99(2), E388.
Qu, K., Wang, Z., Fan, H., Li, J., Liu, J., Li, P., ... & Dong, X. (2017). MCM7 promotes cancer progression through cyclin D1-dependent signaling and serves as a prognostic marker for patients with hepatocellular carcinoma. Cell death & disease, 8(2), e2603.

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