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We have recently reported that Rootletin prevents Cep68 from VHL-mediated proteasomal degradation to maintain centrosome cohesion, unveiling the first underlying mechanism of a linker protein required for maintenance of centrosome cohesion. The minichromosome maintenance (MCM) proteins 2-7 have long been noticed to localize to centrosomes, but their functions at the centrosome are presently unknown. Here, we show that MCM7 directly binds to the centrosomal linker protein Cep68 in vitro and complexes with Cep68 and VHL in vivo. Absence of MCM7 weakened the interaction between Cep68 and VHL, whereas MCM7 overexpression facilitated the Cep68-VHL association. As a result of MCM7 overexpression, Cep68 was targeted for ubiquitination and proteasomal degradation, thereby rendering centrosome splitting. We propose that Cep68 protein level needs to be fine-tuned in order to ensure that its direct interactors, such as the microcephaly protein Cep215 and PCNT, function properly.
The minichromosome maintenance (MCM) proteins are essential for DNA replication initiation and elongation in eukaryotes. In mammalian cells, MCM2-MCM7 complexes are believed to unwind DNA during chromosomal DNA replication. Here we identified a novel MCM family gene, MCM9, by using bioinformatics. Human, mouse, and rat MCM9 showed approximately 90-91% total-amino acid identity. MCM9 showed 24-31% total-amino acid identity with MCM2-MCM8 protein. Phylogenetic analysis on MCM family members revealed that MCM9 was most closely related to MCM8. Human, mouse, and rat MCM9 gene, consisting of 7, 8, and 7 exons, was mapped to 6q22.1-22.33, 10B3, and 20q11, respectively. We identified transcription factor E2F-binding motifs in the vicinity of the transcription start site among human, mouse, and rat MCM9 gene. MCM9 mRNA was upregulated by transcription factor E2E1 and serum stimulation in NIH3T3 cells.
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