Cited by 137DNA Repair MechanismsCancer-related Molecular PathwaysMicrotubule and mitosis dynamics

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Chk1, but not Chk2, inhibits Cdc25 phosphatases by a novel common mechanism.

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Uto, Katsuhiro, Inoue, Daigo, Shimuta, Ken, Nakajo, Nobushige, Sagata, Noriyuki·2004·The EMBO Journal

DOI 10.1038/sj.emboj.7600328PMC PMC514503

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Abstract

Cdc25 phosphatases activate cyclin-dependent kinases (Cdks) and thereby promote cell cycle progression. In vertebrates, Chk1 and Chk2 phosphorylate Cdc25A at multiple N-terminal sites and target it for rapid degradation in response to genotoxic stress. Here we show that Chk1, but not Chk2, phosphorylates Xenopus Cdc25A at a novel C-terminal site (Thr504) and inhibits it from C-terminally interacting with various Cdk-cyclin complexes, including Cdk1-cyclin A, Cdk1-cyclin B, and Cdk2-cyclin E. Strikingly, this inhibition, rather than degradation itself, of Cdc25A is essential for the Chk1-induced cell cycle arrest and the DNA replication checkpoint in early embryos. 14-3-3 proteins bind to Chk1-phosphorylated Thr504, but this binding is not required for the inhibitory effect of Thr504 phosphorylation. A C-terminal site presumably equivalent to Thr504 exists in all known Cdc25 family members from yeast to humans, and its phosphorylation by Chk1 (but not Chk2) can also inhibit all examined Cdc25 family members from C-terminally interacting with their Cdk-cyclin substrates. Thus, Chk1 but not Chk2 seems to inhibit virtually all Cdc25 phosphatases by a novel common mechanism.

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Authors: Uto, K., Inoue, D., Shimuta, K., Nakajo, N., & Sagata, N.
Affiliations: Kyushu University (JP)
Corresponding author: Sagata, Noriyuki
ORCID: Shimuta, Ken
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2004-07-22
Volume: 23
Issue: 16
Pages: 3386-3396
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7600328
PMC: PMC514503
OpenAlex: W2050348418
Cited by: 134
References: 47
Citations by year: 2026: 2 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 4 · 2021: 9 · 2020: 6 · 2019: 5 · 2018: 2 · 2017: 5 · 2016: 4 · 2015: 4 · 2014: 10 · 2013: 9 · 2012: 6
FWCI: 3.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Japan Science and Technology Agency (CREST)
Core Research for Evolutional Science and Technology
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: Chk1, Chk2, CDC25A, Cdc25 phosphatase, cyclin-CDK complexes, CDK1/cyclin B, cyclin E/CDK2, DNA replication checkpoint, cell cycle arrest, 14-3-3 proteins, genotoxic stress, Xenopus embryo
MeSH terms: Checkpoint Kinase 1, Amino Acid Sequence, Animals, DNA Replication, Humans, Molecular Sequence Data, Mutation, Phosphorylation, Phosphothreonine, Protein Binding, Protein Kinases, Xenopus laevis, Cyclins, Sequence Alignment, Protein Serine-Threonine Kinases, cdc25 Phosphatases, Xenopus Proteins, 14-3-3 Proteins, Checkpoint Kinase 2

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Chk1, but not Chk2, inhibits Cdc25 phosphatases by a novel common mechanism.

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