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Knockdown of both HP1a (show CBX5 Proteins) and Mcm10 genes inhibited the progression of S phase in eye imaginal discs. Proximity Ligation Assay (PLA) demonstrated that HP1a (show CBX5 Proteins) is in close proximity to DNA replication proteins including Mcm10, RFC140 (show RFC1 Proteins) and DNA polymerase epsilon 255 kDa subunit in S-phase.
Observation of embryonic nuclear morphology and quantification of embryo hatch rates reveal that maternal loading of Mcm10 is required for embryonic nuclear stability, and suggest a role for Mcm10 post zygotic transition.
Data show that Mcm10 has a role in heterochromatic silencing and chromosome condensation.
Results show that MCM10 is significantly upregulated in urothelial carcinoma (UC), and associated with tumor aggressiveness. Its knockdown significantly suppressed cell proliferation in UC cell lines.
Data suggest that interaction of Mcm10 with Mcm2-7 (show MCM2 Proteins) 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 (show MCM2 Proteins)-binding domain are required for full activity of Mcm10.
RecQL4 (show RECQL4 Proteins)-dependent association of Mcm10 and Ctf4 (show WDHD1 Proteins) with replication origins appears to be the first important step controlled by S phase promoting kinases and checkpoint pathways for the initiation of DNA replication in human cells.
MCM10 is the natural substrate of the Cul4-DDB1[VprBP] E3 ubiquitin ligase whose degradation is regulated by VprBP, but Vpr enhances the proteasomal degradation of MCM10 by interacting with VprBP.
Loss of Mcm10 engages checkpoint, DNA repair and SUMO-dependent rescue pathways that collectively counteract replication stress and chromosome breakage. [Review]
Mcm10 utilizes a modular architecture to act as a replisome scaffold, which helps to define possible roles in origin DNA melting, Pol alpha recruitment and coordination of enzymatic activities during elongation.
Data suggest that CDC45 (show CDC45 Proteins) and MCM10 (minichromosome maintenance complex component 10) directly interact and establish a mutual co-operation in DNA binding; key domains appear to interact and then interact with DNA inside cells or in cell-free systems.
This report shows that human Mcm10 is an acetylated protein regulated by SIRT1 (show SIRT1 Proteins), which binds and deacetylates Mcm10 both in vivo and in vitro, and modulates Mcm10 stability and ability to bind DNA.
High doses of ionizing gamma radiation and exposure to a combination of DNA-damaging chemicals do not decrease Mcm10 protein levels, demonstrating that Mcm10 down-regulation is triggered only by UV-specific damage
human Mcm10 is temporarily recruited to the replication sites 30-60 min before they replicate and dissociates from chromatin after the activation of the prereplication complex
the absence of Mcm10 or its phosphorylation by CDK (show CDK4 Proteins) results in instability of replisome proteins on DNA, which is particularly important under conditions of replication stress.
Dna2 co-localizes in foci with RPA (show RPA1 Proteins) and is found in a complex with replication fork components And-1 and Mcm10. Dna2 interacts with the DSB repair and checkpoint proteins Nbs1 (show NLRP2 Proteins) and ATM (show ATM Proteins).
insight in the action of Mcm10 in the replisome
analysis of domain architecture and biochemical characterization of vertebrate Mcm10
Structural basis for DNA binding by replication initiator Mcm10 is reported.
Genetic evidence for an essential and non-redundant physiological role of MCM10 during murine peri (show POSTN Proteins)-implantation development.
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 it may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein can interact with MCM2 and MCM6, as well as with the origin recognition protein ORC2. It is regulated by proteolysis and phosphorylation in a cell cycle-dependent manner. Studies of a similar protein in Xenopus suggest that the chromatin binding of this protein at the onset of DNA replication is after pre-RC assembly and before origin unwinding. Alternatively spliced transcript variants encoding distinct isoforms have been identified.
, sensitized chromosome inheritance modifier 19
, MCM10 minichromosome maintenance deficient 10
, homolog of yeast MCM10
, protein MCM10 homolog
, minichromosome maintenance deficient 10