ArticleMolecular and cellular biology1999
Cell cycle-dependent regulation of human DNA polymerase alpha-primase activity by phosphorylation.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 85 citations in OpenAlex.
- Switch from canonical to recombination-dependent DNA synthesis by M-CDK phosphorylation of DNA Polα.The EMBO journal · 2026Article
- Mitotic kinase regulation of DNA replication forks.bioRxiv : the preprint server for biology · 2026Article
- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins.International journal of molecular sciences · 2024Article
- Review
- Alterations of cell cycle genes in cancer: unmasking the role of cancer stem cells.Molecular biology reports · 2020Review
- An intact Mcm10 coiled-coil interaction surface is important for origin melting, helicase assembly and the recruitment of Pol-α to Mcm2-7.Nucleic acids research · 2017Article
- Review
- Emerging Roles for Ciz1 in Cell Cycle Regulation and as a Driver of Tumorigenesis.Biomolecules · 2016Review
- Article
- Structural basis for the interaction of a hexameric replicative helicase with the regulatory subunit of human DNA polymerase α-primase.The Journal of biological chemistry · 2012Article
- A distinct first replication cycle of DNA introduced in mammalian cells.Nucleic acids research · 2011Article
- Simian virus 40 activates ATR-Delta p53 signaling to override cell cycle and DNA replication control.Journal of virology · 2010Article
- Structure of a DNA polymerase alpha-primase domain that docks on the SV40 helicase and activates the viral primosome.The Journal of biological chemistry · 2010Article
- Aberrant DNA polymerase alpha is excluded from the nucleus by defective import and degradation in the nucleus.The Journal of biological chemistry · 2009Article
- Phosphorylation of human DNA polymerase lambda by the cyclin-dependent kinase Cdk2/cyclin A complex is modulated by its association with proliferating cell nuclear antigen.Nucleic acids research · 2005Article
- Cell cycle-dependent regulation of a human DNA helicase that localizes in DNA damage foci.Molecular biology of the cell · 2004Article
- Phosphorylation of the PCNA binding domain of the large subunit of replication factor C on Thr506 by cyclin-dependent kinases regulates binding to PCNA.Nucleic acids research · 2003Article
- DNA replication: a complex matter.EMBO reports · 2003Review
- Multiple roles for kinases in DNA replication.EMBO reports · 2003Review
- Role of the p68 subunit of human DNA polymerase alpha-primase in simian virus 40 DNA replication.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
DNA polymerase alpha-primase is known to be phosphorylated in human and yeast cells in a cell cycle-dependent manner on the p180 and p68 subunits. Here we show that phosphorylation of purified human DNA polymerase alpha-primase by purified cyclin A/cdk2 in vitro reduced its ability to initiate simian virus 40 (SV40) DNA replication in vitro, while phosphorylation by cyclin E/cdk2 stimulated its initiation activity. Tryptic phosphopeptide mapping revealed a family of p68 peptides that was modified well by cyclin A/cdk2 and poorly by cyclin E/cdk2. The p180 phosphopeptides were identical with both kinases. By mass spectrometry, the p68 peptide family was identified as residues 141 to 160. Cyclin A/cdk2- and cyclin A/cdc2-modified p68 also displayed a phosphorylation-dependent shift to slower electrophoretic mobility. Mutation of the four putative phosphorylation sites within p68 peptide residues 141 to 160 prevented its phosphorylation by cyclin A/cdk2 and the inhibition of replication activity. Phosphopeptide maps of the p68 subunit of DNA polymerase alpha-primase from human cells, synchronized and labeled in G1/S and in G2, revealed a cyclin E/cdk2-like pattern in G1/S and a cyclin A/cdk2-like pattern in G2. The slower-electrophoretic-mobility form of p68 was absent in human cells in G1/S and appeared as the cells entered G2/M. Consistent with this, the ability of DNA polymerase alpha-primase isolated from synchronized human cells to initiate SV40 replication was maximal in G1/S, decreased as the cells completed S phase, and reached a minimum in G2/M. These results suggest that the replication activity of DNA polymerase alpha-primase in human cells is regulated by phosphorylation in a cell cycle-dependent manner.
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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.