ArticleProceedings of the National Academy of Sciences of the United States of America1996
Phosphorylation of MCM4 by cdc2 protein kinase inhibits the activity of the minichromosome maintenance complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 125 citations in OpenAlex.
- Multi-omics pan-cancer analyses identify MCM4 as a promising prognostic and diagnostic biomarker.Scientific reports · 2024Article
- Review
- Review
- Comprehensive Analysis of the Expression and Prognosis for MCM4 in Uterine Corpus Endometrial Carcinoma.Frontiers in genetics · 2022Article
- Mitotic CDK Promotes Replisome Disassembly, Fork Breakage, and Complex DNA Rearrangements.Molecular cell · 2019Article
- Article
- Cdk1-mediated phosphorylation of Cdc7 suppresses DNA re-replication.Cell cycle (Georgetown, Tex.) · 2016Article
- Visualization of the MCM DNA helicase at replication factories before the onset of DNA synthesis.Chromosoma · 2012Article
- Phosphorylation of MCM3 protein by cyclin E/cyclin-dependent kinase 2 (Cdk2) regulates its function in cell cycle.The Journal of biological chemistry · 2011Article
- Persistent p21 expression after Nutlin-3a removal is associated with senescence-like arrest in 4N cells.The Journal of biological chemistry · 2010Article
- Functional cooperation between FACT and MCM is coordinated with cell cycle and differential complex formation.Journal of biomedical science · 2010Article
- Network architecture of signaling from uncoupled helicase-polymerase to cell cycle checkpoints and trans-lesion DNA synthesis.Cell cycle (Georgetown, Tex.) · 2009Article
- Transient nutlin-3a treatment promotes endoreduplication and the generation of therapy-resistant tetraploid cells.Cancer research · 2008Article
- Interplay between S-cyclin-dependent kinase and Dbf4-dependent kinase in controlling DNA replication through phosphorylation of yeast Mcm4 N-terminal domain.Molecular biology of the cell · 2008Article
- The promoter regions of the Myb-regulated Adora2B and Mcm4 genes co-localize with origins of DNA replication.BMC molecular biology · 2007Article
- Cdt1 revisited: complex and tight regulation during the cell cycle and consequences of deregulation in mammalian cells.Cell division · 2006Article
- Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication.Journal of virology · 2006Article
- The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding.The EMBO journal · 2005Article
- DNA replication and progression through S phase.Oncogene · 2005Review
- Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase.Journal of virology · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotes, tight regulatory mechanisms ensure the ordered progression through the cell cycle phases. The mechanisms that prevent chromosomal DNA replication from taking place more than once each cell cycle are thought to involve the function of proteins of the minichromosome maintenance (MCM) family. Here, we demonstrate that Xenopus MCM4, a member of the MCM protein family related to Spcdc21/ ScCDC54, is part of a large protein complex comprising several other MCM proteins. MCM4 undergoes cell cycle-dependent phosphorylation both in cleaving embryos and in cell-free extracts. MCM4 phosphorylation starts concomitantly with the clearing of the MCM complex from the chromatin during S phase. Phosphorylation is carried out by cdc2/cyclinB protein kinase, which phosphorylates MCM4 in vitro at identical sites as the ones phosphorylated in vivo. Phosphorylation is specific for cdc2 protein kinase since MCM4 is not a substrate for other members of the cdk family. Furthermore, phosphorylation of MCM4 dramatically reduces its affinity for the chromatin. We propose that the cell cycle-dependent phosphorylation of MCM4 is a mechanism which inactivates the MCM complex from late S phase through mitosis, thus preventing illegitimate DNA replication during that period of the cell cycle.
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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.