ArticleNucleic acids research2011
Phosphorylation of Mcm2 modulates Mcm2-7 activity and affects the cell's response to DNA damage.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- MCM2 germline variants predispose to familial papillary thyroid carcinoma due to genomic instability caused by MCM complex disruption.Oncogene · 2026Article
- Antitumor effects of the novel docetaxel derivative JJH201601 in glioma: targeting ribosome biogenesis and enhancing temozolomide sensitivity.Journal of translational medicine · 2026Article
- Review
- Review
- Persistent Acetylation of Histone H3 Lysine 56 Compromises the Activity of DNA Replication Origins.Molecular and cellular biology · 2023Article
- Article
- The Minichromosome Maintenance Complex Component 2 (MjMCM2) of Meloidogyne javanica is a potential effector regulating the cell cycle in nematode-induced galls.Scientific reports · 2022Article
- Dbf4-Dependent Kinase: DDK-ated to post-initiation events in DNA replication.Cell cycle (Georgetown, Tex.) · 2021Review
- Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Review
- Conserved mechanism for coordinating replication fork helicase assembly with phosphorylation of the helicase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mcm2-7 Is an Active Player in the DNA Replication Checkpoint Signaling Cascade via Proposed Modulation of Its DNA Gate.Molecular and cellular biology · 2015Article
- DNA induces conformational changes in a recombinant human minichromosome maintenance complex.The Journal of biological chemistry · 2015Article
- The Dbf4-Cdc7 kinase promotes Mcm2-7 ring opening to allow for single-stranded DNA extrusion and helicase assembly.The Journal of biological chemistry · 2015Article
- Expression of minichromosome maintenance 8 in chronic myelogenous leukemia.International journal of clinical and experimental pathology · 2015Article
- Insights into the Initiation of Eukaryotic DNA Replication.Nucleus (Austin, Tex.) · 2015Article
- Domain within the helicase subunit Mcm4 integrates multiple kinase signals to control DNA replication initiation and fork progression.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dbf4 and Cdc7 proteins promote DNA replication through interactions with distinct Mcm2-7 protein subunits.The Journal of biological chemistry · 2013Article
- Article
- Mcm2 phosphorylation and the response to replicative stress.BMC genetics · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The S-phase kinase, DDK controls DNA replication through phosphorylation of the replicative helicase, Mcm2-7. We show that phosphorylation of Mcm2 at S164 and S170 is not essential for viability. However, the relevance of Mcm2 phosphorylation is demonstrated by the sensitivity of a strain containing alanine at these positions (mcm2(AA)) to methyl methanesulfonate (MMS) and caffeine. Consistent with a role for Mcm2 phosphorylation in response to DNA damage, the mcm2(AA) strain accumulates more RPA foci than wild type. An allele with the phosphomimetic mutations S164E and S170E (mcm2(EE)) suppresses the MMS and caffeine sensitivity caused by deficiencies in DDK function. In vitro, phosphorylation of Mcm2 or Mcm2(EE) reduces the helicase activity of Mcm2-7 while increasing DNA binding. The reduced helicase activity likely results from the increased DNA binding since relaxing DNA binding with salt restores helicase activity. The finding that the ATP site mutant mcm2(K549R) has higher DNA binding and less ATPase than mcm2(EE), but like mcm2(AA) results in drug sensitivity, supports a model whereby a specific range of Mcm2-7 activity is required in response to MMS and caffeine. We propose that phosphorylation of Mcm2 fine-tunes the activity of Mcm2-7, which in turn modulates DNA replication in response to DNA damage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.