Importin β-dependent nuclear import of TopBP1 in ATR–Chk1 checkpoint in Xenopus egg extracts
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TopBP1, a multiple-BRCT-containing protein, plays diverse functions in DNA metabolism including DNA replication, DNA damage response and transcriptional regulation. The cytoplasmic localization of TopBP1 has been found to be associated with breast cancer susceptibility in clinical studies, suggesting the biological significance of TopBP1's sub-cellular localization. However, it remains elusive how TopBP1 is shuttled into nucleus and recruited to chromatin under normal or stressful conditions. Taking advantage of Xenopus egg extract, we identified Importin β as a new interacting protein of the TopBP1 C-terminus. We verified the TopBP1-Importin β association via GST pulldown and coimmunoprecipitation assays. We then demonstrated that TopBP1's C-terminal motif (designated as CTM, 23 amino acids) containing a putative NLS (nuclear localization signal) was required for Importin β interaction and that CT100 of Importin β (100 amino acids of extreme C-terminus of Importin β) was required for TopBP1 interaction. Further structure-function analysis reveals that the CTM of TopBP1 is essential for TopBP1's nuclear import and subsequent chromatin recruitment, thereby playing important roles in DNA replication and mitomycin C (MMC)-induced Chk1 phosphorylation. In addition, Importin β-specific inhibitor importazole inhibits TopBP1's nuclear import and the MMC-induced Chk1 phosphorylation. With ongoing DNA replication, the Importin β-dependent nuclear import of TopBP1 was indeed required for the MMC-induced Chk1 phosphorylation. Our data also suggest that checkpoint activation requires more TopBP1 than DNA replication does. The requirement of TopBP1's CTM motif for ATR-Chk1 checkpoint can be bypassed in a nucleus-free AT70 system. Taken together, our findings suggest that the CTM motif-mediated TopBP1 shuttling into nucleus via Importin β plays an important role in the ATR-Chk1 checkpoint signaling in Xenopus egg extracts.
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Chk1 is phosphorylated at serine 345 by ATR in response to stalled DNA replication forks and DNA damage induced by UV, ionizing radiation, methyl methanesulfonate, mitomycin C, and hydrogen peroxide.
“As a critical player in DDR, Chk1 is phosphorylated at Serine 345 by ATR in response to stalled DNA replication forks and DNA damage induced by UV, IR, methyl methanesulfonate (MMS), mitomycin C (MMC), and hydrogen peroxide [85–90].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [90]
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- Authors
- Bai, L., Michael, W. M., & Yan, S.
- Affiliations
- University of North Carolina at Charlotte (US)
- University of Southern California (US)
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2014-05
- Volume
- 26
- Issue
- 5
- Pages
- 857-867
- ISSN
- 0898-6568 (ISSN-L)
- PMC
- PMC3951582
- OpenAlex
- W2057925576
- Cited by
- 19
- References
- 76
- Citations by year
- 2024: 2 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 1
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cellular Signalling (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of North Carolina at Charlotte
- NIH/NIGMS (R15 GM101571, R01 GM067735)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- TopBP1, importin beta, nuclear import, nuclear localization signal, chromatin recruitment, DNA replication, Chk1 phosphorylation, mitomycin C, BRCT domain, Xenopus egg extracts, checkpoint signaling
- MeSH terms
- Checkpoint Kinase 1, Amino Acid Sequence, Animals, Carrier Proteins, Cell Nucleus, DNA Repair, DNA-Binding Proteins, Molecular Sequence Data, Ovum, Phosphorylation, Protein Kinases, Quinazolines, Xenopus laevis, Signal Transduction, Mitomycin, Protein Structure, Secondary, Protein Structure, Tertiary, Amino Acid Motifs, Active Transport, Cell Nucleus, beta Karyopherins, Xenopus Proteins, Ataxia Telangiectasia Mutated Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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