MCM2

Official Full Name

minichromosome maintenance complex component 2

Organism

Homo sapiens

GeneID

4171

Background

The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in 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. This protein forms a complex with MCM4, 6, and 7, and has been shown to regulate the helicase activity of the complex. This protein is phosphorylated, and thus regulated by, protein kinases CDC2 and CDC7. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined. [provided by RefSeq, Oct 2012]

Synonyms

BM28; CCNL1; CDCL1; cdc19; DFNA70; D3S3194; MITOTIN;

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Detailed Information

MCM2 is a member of the minichromosome maintenance protein family. MCM2 was previously named CCNL1, BM28, and CDCL1. It plays an important role in DNA replication initiation and replication fork movement. It is closely related to cell proliferation and is a good indicator for studying tumor cell growth and evaluating the prognosis of some tumors. The MCMs protein is a nuclear protein family of six subunits, MCM2, MCM3, MCM4 (Cdc21), MCM5 (Cdc46), MCM6 (Mis5), and MCM7 (Cdc47), which have similar biological effects and play an equally important role in the process in beginning and extension of the DNA replication.

The Role of MCM2

MCM2 content is very low in quiescent cells. In proliferating and transformed cells, MCM2 content begins to increase in G1 phase, peaks in early G1 and early S, and binds to chromatin. In the S phase to the M phase, it is free MCM2, and it is decreased in the G2 phase and the M phase. Due to this cyclical change consistent with the cell proliferation process, it has been regarded as a marker of S phase cells, that is, expressed only in proliferating cells, and is considered to be a specific proliferation-related factor, and is considered to be the sign of precancerous. The level of MCM protein can be directly reflected by detecting MCM2. Therefore, MCM2 is a good indicator for studying tumor cell motility and evaluating the prognosis of some tumors. MCM2 has also been reported that it may play a role in acute myeloid leukemia.

Figure 1. Multiple Functions for Mcm2–7 ATPase Motifs during Replication Initiation. （Kang, et al. 2014）

MCM2 protein can better distinguish corresponding normal tissues, atypical hyperplasia tissues and tumor tissues, and can be used as an important biomarker for malignant tumors and dysplasia. It is a cell proliferation marker superior to proliferating cell nuclear antigen (PCNA) and Ki-67. Because PCNA is also expressed in repair cells, it affects the accuracy of PCNA reflecting cell proliferation activity; Ki-67 is not expressed in early G1, so it cannot fully reflect cell proliferation activity. MCM (including MCM2) is expressed only in cells in the proliferative cycle and can accurately and comprehensively reflect cell proliferation activity. The absence of MCM protein means that the cell has withdrawn from the proliferative cycle, becomes a differentiated mature cell or enters the G0 phase, and thus can be used as a valid indicator for determining the prognosis of the tumor.

MCM2 Protein and Cancer

Immunohistochemistry was used to detect the expression of protein MCM2 and Ki-67 in 221 cases of non-small-celllungcancer (NSCLC) tumor samples, and the regression analysis was performed on the experimental results, pathological features, clinical manifestations and survival. The study found that the stage and location of the tumor and the MCM2 staining level were significantly correlated with survival, and the MCM2 positive staining rate. MCM2 is not only highly expressed in breast cancer tissues, but also significantly associated with prognosis. The study found that MCM2 was positively correlated between normal breast (P = 0.0003) and breast cancer (P < 0.0001).

The expression of MCM2 and Ki-67 in surgically resected tumor specimens of 93 patients with esophageal squamous cell carcinoma was detected by immunohistochemistry. It was found that MCM2 was mainly expressed in the nucleus, and its expression index (LI) in esophageal squamous cell carcinoma was significantly higher than that of normal squamous epithelium (P<0.0001). MCM2 may be more reliable and effective than Ki67 in evaluating the prognosis, tumor infiltration, and tumor cell growth in patients with esophageal squamous cell carcinoma.

References:

Cheung, C. H. Y. , Hsu, C. L. , Chen, K. P. , Chong, S. T. , Wu, C. H. , & Huang, H. C. , et al. (2017). Mcm2-regulated functional networks in lung cancer by multi-dimensional proteomic approach. Scientific Reports, 7(1), 13302.
Feng, J. , Liang, J. , Li, J. , Li, Y. , Liang, H. , & Zhao, X. , et al. (2015). Pten controls the dna replication process through mcm2 in response to replicative stress. Cell Reports, 13(7), 1295-1303.
Kang, S. , Warner, M. , & Bell, S. . (2014). Multiple functions for mcm2–7 atpase motifs during replication initiation. Molecular Cell, 55(5), 655-665.

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