Cited by 157DNA Repair MechanismsCancer-related Molecular PathwaysBRCA gene mutations in cancer

The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.

Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation

Open access

Lin, Shiaw-Yih, Li, Kaiyi, Stewart, Grant S., Elledge, Stephen J.·2004·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0401847101PMC PMC404071

Open this paper in CoChat — free account

Abstract

Claspin is a homolog of Mrc1, a checkpoint protein required for the DNA replication checkpoint in yeast. In Xenopus , phosphorylated Claspin binds to xChk1 and regulates xChk1 activation in response to replication stress. In this study, we have shown that the human homolog of Claspin is required for resistance to multiple forms of genotoxic stress including UV, IR, and hydroxyurea. Phosphorylation of Claspin was found to depend on the ataxia telangiectasia mutated-Rad3 related (ATR) pathway. DNA damage induces the formation of a complex between Claspin and BRCA1, a second regulator of Chk1 activation. Claspin was found to control BRCA1 phosphorylation on serine 1524, a site whose phosphorylation is controlled by the ATR pathway. These results are consistent with a model in which ATR regulates Claspin phosphorylation in response to DNA damage and replication stress resulting in recruitment and phosphorylation of BRCA1. BRCA1 and Claspin then function to activate the tumor suppressor Chk1. Unexpectedly, we found that Claspin has a second, positive role in control of the cell cycle as Claspin overexpression increased cell proliferation. These results suggest that Claspin has properties of both a tumor suppressor and an oncogene.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.0401847101

Cites

27 of 27 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Sensing DNA Damage Through ATRIP Recognition of RPA-ssDNA Complexes
Zou, L., & Elledge, S. J. (2003) · Science · doi:10.1126/science.1083430 · Cited by 2,693
Self-citation
Cell cycle checkpoint signaling through the ATM and ATR kinases
Abraham, R. T. (2001) · Genes & Development · doi:10.1101/gad.914401 · Cited by 1,966
Chk1 is an essential kinase that is regulated by Atr and required for the G 2 /M DNA damage checkpoint
Liu, Q., Guntuku, S., Cui, X.-S., Matsuoka, S., Cortez, D., Tamai, K., Luo, G., Carattini-Rivera, S., DeMayo, F., Bradley, A., et al. (2000) · Genes & Development · doi:10.1101/gad.14.12.1448 · Cited by 1,625
Self-citation
Linkage of ATM to Cell Cycle Regulation by the Chk2 Protein Kinase
Matsuoka, S. (1998) · Science · doi:10.1126/science.282.5395.1893 · Cited by 1,322
Conservation of the Chk1 Checkpoint Pathway in Mammals: Linkage of DNA Damage to Cdk Regulation Through Cdc25
Sanchez, Y., Wong, C., Thoma, R. S., Richman, R., Wu, Z., Piwnica-Worms, H., & Elledge, S. J. (1997) · Science · doi:10.1126/science.277.5331.1497 · Cited by 1,320
Self-citation
Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro
Matsuoka, S., Rotman, G., Ogawa, A., Shiloh, Y., Tamai, K., & Elledge, S. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.190030497 · Cited by 849
Self-citation
Radiosensitivity in ataxia-telangiectasia: a new explanation.
Painter, R. B., & Young, B. R. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7315 · Cited by 795
A splicing mutation affecting expression of ataxia–telangiectasia and Rad3–related protein (ATR) results in Seckel syndrome
O'Driscoll, M., Ruiz-Perez, V. L., Woods, C. G., Jeggo, P. A., & Goodship, J. A. (2003) · Nature Genetics · doi:10.1038/ng1129 · Cited by 794
S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex
Katou, Y., Kanoh, Y., Bando, M., Noguchi, H., Tanaka, H., Ashikari, T., Sugimoto, K., & Shirahige, K. (2003) · Nature · doi:10.1038/nature01900 · Cited by 649
ATM and ATR: networking cellular responses to DNA damage
Shiloh, Y. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00159-3 · Cited by 601

Show all 27 references

Sorted by citations

Cell-cycle checkpoints and cancer
Kastan, M. B., & Bartek, J. (2004) · Nature · doi:10.1038/nature03097 · Cited by 2,836
TopBP1 Activates the ATR-ATRIP Complex
Kumagai, A., Lee, J., Yoo, H. Y., & Dunphy, W. G. (2006) · Cell · doi:10.1016/j.cell.2005.12.041 · Cited by 787
Initiating Cellular Stress Responses
Bakkenist, C. J., & Kastan, M. B. (2004) · Cell · doi:10.1016/j.cell.2004.06.023 · Cited by 544
Eukaryotic Chromosome DNA Replication: Where, When, and How?
Masai, H., Matsumoto, S., You, Z., Yoshizawa-Sugata, N., & Oda, M. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.103205 · Cited by 524
The Cdc14B-Cdh1-Plk1 Axis Controls the G2 DNA-Damage-Response Checkpoint
Bassermann, F., Frescas, D., Guardavaccaro, D., Busino, L., Peschiaroli, A., & Pagano, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.043 · Cited by 397
A Role for the Deubiquitinating Enzyme USP28 in Control of the DNA-Damage Response
Zhang, D., Zaugg, K., Mak, T. W., & Elledge, S. J. (2006) · Cell · doi:10.1016/j.cell.2006.06.039 · Cited by 328
Self-citation
Phase I Study of Single-Agent AZD1775 (MK-1775), a Wee1 Kinase Inhibitor, in Patients With Refractory Solid Tumors
Do, K. T., Wilsker, D. F., Ji, J. J., Zlott, J., Freshwater, T., Kinders, R. J., Collins, J. M., Chen, A. P., Doroshow, J. H., & Kummar, S. (2015) · Journal of Clinical Oncology · doi:10.1200/jco.2014.60.4009 · Cited by 327
SCFβTrCP-Mediated Degradation of Claspin Regulates Recovery from the DNA Replication Checkpoint Response
Peschiaroli, A., Dorrello, N. V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N. E., & Pagano, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.013 · Cited by 289
The Rad9-Hus1-Rad1 Checkpoint Clamp Regulates Interaction of TopBP1 with ATR
Lee, J., Kumagai, A., & Dunphy, W. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704635200 · Cited by 294
Destruction of Claspin by SCFβTrCP Restrains Chk1 Activation and Facilitates Recovery from Genotoxic Stress
Mailand, N., Bekker-Jensen, S., Bartek, J., & Lukas, J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.016 · Cited by 258
Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress
Yan, S., Sorrell, M., & Berman, Z. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1666-4 · Cited by 247
The Human Tim/Tipin Complex Coordinates an Intra-S Checkpoint Response to UV That Slows Replication Fork Displacement
Ünsal-Kaçmaz, K., Chastain, P. D., Qu, P.-P., Minoo, P., Cordeiro-Stone, M., Sancar, A., & Kaufmann, W. K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02190-06 · Cited by 240
SQ/TQ cluster domains: concentrated ATM/ATR kinase phosphorylation site regions in DNA-damage-response proteins
Traven, A., & Heierhorst, J. (2005) · BioEssays · doi:10.1002/bies.20204 · Cited by 224
DNA replication and progression through S phase
Takeda, D. Y., & Dutta, A. (2005) · Oncogene · doi:10.1038/sj.onc.1208616 · Cited by 201
Functions, Regulation, and Therapeutic Implications of the ATR Checkpoint Pathway
Yazinski, S. A., & Zou, L. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-121415-121658 · Cited by 178
Evidence That the ATR/Chk1 Pathway Maintains Normal Replication Fork Progression during Unperturbed S Phase
Petermann, E., & Caldecott, K. W. (2006) · Cell Cycle · doi:10.4161/cc.5.19.3256 · Cited by 170
Mechanisms of replication fork protection: a safeguard for genome stability
Errico, A., & Costanzo, V. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.655374 · Cited by 159
The E2F-Regulated Gene Chk1 Is Highly Expressed in Triple-Negative Estrogen Receptor−/Progesterone Receptor−/HER-2− Breast Carcinomas
Verlinden, L., Bempt, I. V., Eelen, G., Drijkoningen, M., Verlinden, I., Marchal, K., Wolf‐Peeters, C. D., Christiaens, M.-R., Michiels, L., Bouillon, R., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3545 · Cited by 149
Chk1-Mediated Phosphorylation of FANCE Is Required for the Fanconi Anemia/BRCA Pathway
Wang, X., Kennedy, R. D., Ray, K., Stuckert, P., Ellenberger, T., & D’Andrea, A. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02357-06 · Cited by 147
Overexpression of Claspin and Timeless protects cancer cells from replication stress in a checkpoint-independent manner
Bianco, J. N., Bergoglio, V., Lin, Y., Pillaire, M., Schmitz, A.-L., Gilhodes, J., Lusque, A., Mazières, J., Lacroix‐Triki, M., Roumeliotis, T. I., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08886-8 · Cited by 150
Maintenance of fork integrity at damaged DNA and natural pause sites
Tourrière, H., & Pasero, P. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.02.004 · Cited by 151
Rad17 Phosphorylation Is Required for Claspin Recruitment and Chk1 Activation in Response to Replication Stress
Wang, X., Zou, L., Lu, T., Bao, S., Hurov, K. E., Hittelman, W. N., Elledge, S. J., & Li, L. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.022 · Cited by 138
Self-citation
Human Tim/Timeless-interacting Protein, Tipin, Is Required for Efficient Progression of S Phase and DNA Replication Checkpoint
Yoshizawa-Sugata, N., & Masai, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605596200 · Cited by 127
Tipin-Replication Protein A Interaction Mediates Chk1 Phosphorylation by ATR in Response to Genotoxic Stress
Kemp, M. G., Akan, Z., Yilmaz, S., Grillo, M., Smith‐Roe, S. L., Kang, T., Cordeiro‐Stone, M., Kaufmann, W. K., Abraham, R. T., Sancar, A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110304 · Cited by 129
Claspin Promotes Normal Replication Fork Rates in Human Cells
Petermann, E., Helleday, T., & Caldecott, K. W. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1035 · Cited by 116
Sensing, signaling, and responding to DNA damage: Organization of the checkpoint pathways in mammalian cells
Li, L., & Zou, L. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20355 · Cited by 117
DNA-dependent phosphorylation of Chk1 and Claspin in a human cell-free system
Clarke, C., & Clarke, P. R. (2005) · Biochemical Journal · doi:10.1042/bj20041966 · Cited by 108
Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis
Richard, D. J., Bolderson, E., & Khanna, K. K. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230902849180 · Cited by 108
Human Papillomavirus 16 E7 Oncoprotein Attenuates DNA Damage Checkpoint Control by Increasing the Proteolytic Turnover of Claspin
Spardy, N. A., Covella, K., Cha, E., Hoskins, E. E., Wells, S. I., Duensing, A. U., & Duensing, S. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0925 · Cited by 104
Targeting deubiquitinase USP28 for cancer therapy
Wang, X., Liu, Z., Zhang, L., Yang, Z., Chen, X., Luo, J., Zhou, Z., Mei, X., Yu, X., Shao, Z., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0208-z · Cited by 102
Cdc7 kinase mediates Claspin phosphorylation in DNA replication checkpoint
Kim, J. M., Kakusho, N., Yamada, M., Kanoh, Y., Takemoto, N., & Masai, H. (2007) · Oncogene · doi:10.1038/sj.onc.1210994 · Cited by 98
Ependymoma gene expression profiles associated with histological subtype, proliferation, and patient survival
Zangen, I. L.-V., Kneitz, S., Monoranu, C., Rutkowski, S., Hinkes, B. G., Vince, G. H., Huang, B., & Roggendorf, W. (2007) · Acta Neuropathologica · doi:10.1007/s00401-006-0190-5 · Cited by 94
Phosphatases in the cellular response to DNA damage
Freeman, A. K., & Monteiro, Á. N. A. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-27 · Cited by 104
Tipin is required for stalled replication forks to resume DNA replication after removal of aphidicolin in Xenopus egg extracts
Errico, A., Costanzo, V., & Hunt, T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706347104 · Cited by 92
Human Claspin Is a Ring-shaped DNA-binding Protein with High Affinity to Branched DNA Structures
Sar, F., Lindsey‐Boltz, L. A., Subramanian, D., Croteau, D. L., Hutsell, S. Q., Griffith, J. D., & Sancar, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405793200 · Cited by 86
Viral and cellular interactions during adenovirus DNA replication
Charman, M., Herrmann, C., & Weitzman, M. D. (2019) · FEBS Letters · doi:10.1002/1873-3468.13695 · Cited by 82
Repeated Phosphopeptide Motifs in Human Claspin Are Phosphorylated by Chk1 and Mediate Claspin Function
Chini, C. C. S., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604373200 · Cited by 78
DNA Structure and Integrity Checkpoints during the Cell Cycle and Their Role in Drug Targeting and Sensitivity of Tumor Cells to Anticancer Treatment
Składanowski, A., Bozko, P. M., & Sabisz, M. (2009) · Chemical Reviews · doi:10.1021/cr900026u · Cited by 74
Checkpoint adaptation in human cells
Syljuåsen, R. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210402 · Cited by 78
Roles of Replication Fork-interacting and Chk1-activating Domains from Claspin in a DNA Replication Checkpoint Response
Lee, J., Gold, D. A., Shevchenko, A., Shevchenko, A., & Dunphy, W. G. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0671 · Cited by 72
The S phase checkpoint: When the crowd meets at the fork
Gottifredi, V., & Prives, C. L. (2005) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2005.02.011 · Cited by 68
Identifying Host Factors Associated with DNA Replicated During Virus Infection
Reyes, E. D., Kulej, K., Pancholi, N. J., Akhtar, L. N., Avgousti, D. C., Kim, E. T., Bricker, D. K., Spruce, L. A., Koniski, S. A., Seeholzer, S. H., et al. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m117.067116 · Cited by 67
HERC2/USP20 coordinates CHK1 activation by modulating CLASPIN stability
Zhu, M., Zhao, H., Liao, J., & Xu, X. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku978 · Cited by 66
A DNA-Damage Selective Role for BRCA1 E3 Ligase in Claspin Ubiquitylation, CHK1 Activation, and DNA Repair
Sato, K., Sundaramoorthy, E., Rajendra, E., Hattori, H., Jeyasekharan, A. D. D., Ayoub, N., Schiess, R., Aebersold, R. H., Nishikawa, H., Sedukhina, A. S., et al. (2012) · Current Biology · doi:10.1016/j.cub.2012.07.034 · Cited by 67
Chk1 is required to maintain Claspin stability
Chini, C. C. S., Wood, J., & Chen, J. (2006) · Oncogene · doi:10.1038/sj.onc.1209447 · Cited by 62
A ruthenium polypyridyl intercalator stalls DNA replication forks, radiosensitizes human cancer cells and is enhanced by Chk1 inhibition
Gill, M. R., Harun, S. N., Halder, S., Boghozian, R. A., Ramadan, K., Ahmad, H., & Vallis, K. A. (2016) · Scientific Reports · doi:10.1038/srep31973 · Cited by 58
Site-specific phosphorylation of a checkpoint mediator protein controls its responses to different DNA structuresPreprint
Yoo, H. Y., Jeong, S., & Dunphy, W. G. (2006) · Genes & Development · doi:10.1101/gad.1398806 · Cited by 58
Reconstitution of Human Claspin-mediated Phosphorylation of Chk1 by the ATR (Ataxia Telangiectasia-mutated and Rad3-related) Checkpoint Kinase
Lindsey‐Boltz, L. A., Serçin, Ö., Choi, J.-H., & Sancar, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.064485 · Cited by 55
The Deubiquitinase USP9X Maintains DNA Replication Fork Stability and DNA Damage Checkpoint Responses by Regulating CLASPIN during S-Phase
McGarry, E., Gaboriau, D. C. A., Rainey, M. D., Restuccia, U., Bachi, A., & Santocanale, C. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2890 · Cited by 54
Spy1 Expression Prevents Normal Cellular Responses to DNA Damage
Gastwirt, R. F., Slavin, D. A., McAndrew, C. W., & Donoghue, D. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604720200 · Cited by 52
The BRCA1 ubiquitin ligase and homologous recombination repair
Ohta, T., Sato, K., & Wu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.005 · Cited by 53
The human intra-S checkpoint response to UVC-induced DNA damage
Kaufmann, W. K. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp230 · Cited by 56
The BRCA1/BARD1 ubiquitin ligase and its substrates
Witus, S. R., Stewart, M. D., & Klevit, R. E. (2021) · Biochemical Journal · doi:10.1042/bcj20200864 · Cited by 54
Overactive BRCA1 Affects Presenilin 1 in Induced Pluripotent Stem Cell-Derived Neurons in Alzheimer’s Disease
Wężyk, M., Szybińska, A., Wojsiat, J., Szczerba, M., Day, K., Rönnholm, H., Kele, M., Berdyński, M., Pepłońska, B., Fichna, J. P., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170830 · Cited by 51
Claspin recruits Cdc7 kinase for initiation of DNA replication in human cells
Yang, C.-C., Suzuki, M., Yamakawa, S., Uno, S., Ishii, A., Yamazaki, S., Fukatsu, R., Fujisawa, R., Sakimura, K., Tsurimoto, T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12135 · Cited by 50
Fanconi anemia proteins and endogenous stresses
Pang, Q., & Andreassen, P. R. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.03.013 · Cited by 49
The Protective Role of Dormant Origins in Response to Replicative Stress
Courtot, L., Hoffmann, J., & Bergoglio, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113569 · Cited by 57
BRCA1 promotes the ubiquitination of PCNA and recruitment of translesion polymerases in response to replication blockade
Tian, F., Sharma, S., Zou, J., Lin, S., Wang, B., Rezvani, K. S., Wang, H., Parvin, J. D., Ludwig, T., Canman, C. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306534110 · Cited by 48
Self-citation
Cleavage of Claspin by Caspase-7 during Apoptosis Inhibits the Chk1 Pathway
Clarke, C., Bennett, L. N., & Clarke, P. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506460200 · Cited by 46
Mechanisms of ATR-mediated checkpoint signalling
Smits, V. A. J. (2010) · Frontiers in bioscience · doi:10.2741/3649 · Cited by 46
Cleavage and degradation of Claspin during apoptosis by caspases and the proteasome
Semple, J. I., Smits, V. A. J., Hernandez-Fernaud, J. R., Mamely, I., & Freire, R. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402134 · Cited by 45
HERC2 Interacts with Claspin and Regulates DNA Origin Firing and Replication Fork Progression
Izawa, N., Wu, W., Sato, K., Nishikawa, H., Kato, A., Boku, N., Itoh, F., & Ohta, T. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-0385 · Cited by 45
Lack of Bcl11b tumor suppressor results in vulnerability to DNA replication stress and damages
Kamimura, K., Mishima, Y., Obata, M., Endo, T., Aoyagi, Y., & Kominami, R. (2007) · Oncogene · doi:10.1038/sj.onc.1210388 · Cited by 45
Claspin functions in cell homeostasis—A link to cancer?
Azenha, D., Lopes, M. C., & Martins, T. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.09.002 · Cited by 43
Cdc7 activates replication checkpoint by phosphorylating the Chk1-binding domain of Claspin in human cells
Yang, C.-C., Kato, H., Shindo, M., & Masai, H. (2019) · eLife · doi:10.7554/elife.50796 · Cited by 43
Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1
Meng, Z., Capalbo, L., Glover, D. M., & Dunphy, W. G. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-01-0048 · Cited by 41
CtIP, a candidate tumor susceptibility gene is a team player with luminaries
Chinnadurai, G. (2005) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2005.09.002 · Cited by 43
CRL Ubiquitin Ligases and DNA Damage Response
Li, J.-M., & Jin, J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00029 · Cited by 43
Regulation of Claspin degradation by the ubiquitin‐proteosome pathway during the cell cycle and in response to ATR‐dependent checkpoint activation
Bennett, L. N., & Clarke, P. R. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.06.071 · Cited by 39
Cdc7-dependent and -independent phosphorylation of Claspin in the induction of the DNA replication checkpoint
Rainey, M. D., Harhen, B., Wang, G., Murphy, P. V., & Santocanale, C. (2013) · Cell Cycle · doi:10.4161/cc.24675 · Cited by 37
Claspin overexpression is associated with high‐grade histology and poor prognosis in renal cell carcinoma
Kobayashi, G., Sentani, K., Babasaki, T., Sekino, Y., Shigematsu, Y., Hayashi, T., Oue, N., Teishima, J., Matsubara, A., Sasaki, N., et al. (2020) · Cancer Science · doi:10.1111/cas.14299 · Cited by 36
Evaluation of claspin as a proliferation marker in human cancer and normal tissues
Tsimaratou, K., Kletsas, D., Kastrinakis, N. G., Tsantoulis, P. K., Evangelou, K., Sideridou, M., Liontos, M., Poulias, I., Venere, M., Salmas, M., et al. (2006) · The Journal of Pathology · doi:10.1002/path.2095 · Cited by 35
Tethering DNA Damage Checkpoint Mediator Proteins Topoisomerase IIβ-binding Protein 1 (TopBP1) and Claspin to DNA Activates Ataxia-Telangiectasia Mutated and RAD3-related (ATR) Phosphorylation of Checkpoint Kinase 1 (Chk1)
Lindsey‐Boltz, L. A., & Sancar, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237958 · Cited by 36
BRCA1 haploinsufficiency promotes chromosomal amplification under Fenton reaction-based carcinogenesis through ferroptosis-resistance
Kong, Y., Akatsuka, S., Motooka, Y., Zheng, H., Cheng, Z., Shiraki, Y., Mashimo, T., Imaoka, T., & Toyokuni, S. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102356 · Cited by 34
Germline alterations in the CLSPN gene in breast cancer families
Erkko, H., Pylkäs, K., Karppinen, S., & Winqvist, R. (2008) · Cancer Letters · doi:10.1016/j.canlet.2007.11.003 · Cited by 33
The TIMELESS effort for timely DNA replication and protection
Patel, J. A., & Kim, H. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04738-3 · Cited by 33
Characterization of functional domains in human Claspin
Serçin, Ö., & Kemp, M. G. (2011) · Cell Cycle · doi:10.4161/cc.10.10.15562 · Cited by 33
FANCJ/BRIP1 recruitment and regulation of FANCD2 in DNA damage responses
Zhang, F., Fan, Q., Ren, K., Auerbach, A. D., & Andreassen, P. R. (2010) · Chromosoma · doi:10.1007/s00412-010-0285-6 · Cited by 31
Overexpression of claspin promotes docetaxel resistance and is associated with prostate‐specific antigen recurrence in prostate cancer
Babasaki, T., Sentani, K., Sekino, Y., Kobayashi, G., Phạm, Q. T., Katsuya, N., Akabane, S., Taniyama, D., Hayashi, T., Shiota, M., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.4113 · Cited by 30
Clinicopathological significance of claspin overexpression and its efficacy as a novel biomarker for the diagnosis of urothelial carcinoma
Kobayashi, G., Hayashi, T., Sentani, K., Babasaki, T., Sekino, Y., Inoue, S., Uraoka, N., Hanamoto, M., Nose, H., Teishima, J., et al. (2021) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-021-03239-7 · Cited by 29
Molecular Mechanisms of DNA Replication Checkpoint Activation
Recolin, B., van der Laan, S., Tsanov, N., & Maiorano, D. (2014) · Genes · doi:10.3390/genes5010147 · Cited by 34
Antiproliferative chromone derivatives induce K562 cell death through endogenous and exogenous pathways
Jiao, R., Xu, F., Huang, X., Li, H., Liu, W., Cao, H., Zang, L., Li, Z., Hua, H., & Li, D. (2020) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2020.1740696 · Cited by 29
The Adaptive Mechanisms and Checkpoint Responses to a Stressed DNA Replication Fork
Saldanha, J., Rageul, J., Patel, J. A., & Kim, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310488 · Cited by 28
Clinicopathological significance of claspin overexpression and its association with spheroid formation in gastric cancer
Kobayashi, G., Sentani, K., Hattori, T., Yamamoto, Y., Imai, T., Sakamoto, N., Kuraoka, K., Oue, N., Sasaki, N., Taniyama, K., et al. (2018) · Human Pathology · doi:10.1016/j.humpath.2018.09.001 · Cited by 27
Human INT6 interacts with MCM7 and regulates its stability during S phase of the cell cycle
Buchsbaum, S., Morris, C., Bochard, V., & Jalinot, P. (2007) · Oncogene · doi:10.1038/sj.onc.1210314 · Cited by 26
Role of Claspin in regulation of nucleotide excision repair factor DDB2
Prætorius-Ibba, M., Wang, Q.-E., Wani, G., El-Mahdy, M. A., Zhu, Q., Qin, S., & Wani, A. A. (2007) · DNA Repair · doi:10.1016/j.dnarep.2006.11.009 · Cited by 24
Prevalence and Functional Analysis of Sequence Variants in the ATR Checkpoint Mediator Claspin
Zhang, J., Song, Y., Brannigan, B. W., Wahrer, D. C. R., Schiripo, T. A., Harris, P. L., Haserlat, S. M., Ulkus, L. E., Shannon, K., Garber, J. E., et al. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0033 · Cited by 27
The GANT61, a GLI Inhibitor, Induces Caspase-Independent Apoptosis of SK-N-LO Cells
Μatsumoto, T., Tabata, K., & Suzuki, T. (2014) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b13-00920 · Cited by 22
Checkpoint and Coordinated Cellular Responses to DNA Damage
Yang, X. H., & Zou, L. (2006) · Springer eBooks · doi:10.1007/b136684 · Cited by 20
Implications of CLSPN Variants in Cellular Function and Susceptibility to Cancer
Azenha, D., Hernández-Pérez, S., Martín, Y., Viegas, M. S., Martins, A., Lopes, M. C., Lam, E. W. ‐., Freire, R., & Martins, T. (2020) · Cancers · doi:10.3390/cancers12092396 · Cited by 19
The Human Tim-Tipin Complex Interacts Directly with DNA Polymerase ϵ and Stimulates Its Synthetic Activity
Aria, V., Felice, M. D., Perna, R. D., Uno, S., Masai, H., Syväoja, J. E., van Loon, B., Hübscher, U., & Pisani, F. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.398073 · Cited by 19
Phosphoprotein pathway profiling of ovarian carcinoma for the identification of potential new targets for therapy
Faratian, D., Um, I., Wilson, D. S., Mullen, P., Langdon, S. P., & Harrison, D. J. (2011) · European Journal of Cancer · doi:10.1016/j.ejca.2011.01.014 · Cited by 19
Mammalian DNA Damage Response Pathway
Lou, Z., & Chen, J. (2006) · Springer eBooks · doi:10.1007/1-4020-3764-3_15 · Cited by 19
In my end is my beginning: control of end resection and DSBR pathway ‘choice’ by cyclin-dependent kinases
Scully, R., & Xie, A. (2005) · Oncogene · doi:10.1038/sj.onc.1208609 · Cited by 19
Mrc1/Claspin: a new role for regulation of origin firing
Masai, H., Yang, C.-C., & Matsumoto, S. (2017) · Current Genetics · doi:10.1007/s00294-017-0690-y · Cited by 18
Kv10.1 Regulates Microtubule Dynamics during Mitosis
Movsisyan, N., & Pardo, L. A. (2020) · Cancers · doi:10.3390/cancers12092409 · Cited by 18
Structure and function of the highly homologous deubiquitinases ubiquitin specific peptidase 25 and 28: Insights into their pathophysiological and therapeutic roles
Zhou, L., Qin, B., Yassine, D. M., Luo, M., Liu, X., Wang, F., & Wang, Y. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115624 · Cited by 17
Protein Kinases That Regulate Chromosome Stability and Their Downstream Targets
Nojima, H. (2006) · KARGER eBooks · doi:10.1159/000092505 · Cited by 17
BRCA1 Is Required for Maintenance of Phospho-Chk1 and G2/M Arrest during DNA Cross-Link Repair in DT40 Cells
Draga, M., Madgett, E. B., Vandenberg, C. J., du Plessis, D., Kaufmann, A., Werler, P., Chakraborty, P., Lowndes, N. F., & Hiom, K. J. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01497-14 · Cited by 18
Posttranscriptional control of the replication stress response via TTP-mediated Claspin mRNA stabilization
Lee, T.-H., Choi, J. Y., Park, J., & Kang, T. (2020) · Oncogene · doi:10.1038/s41388-020-1220-9 · Cited by 16

Authors: Lin, S.-Y., Li, K., Stewart, G. S., & Elledge, S. J.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Lin, Shiaw-Yih
Li, Kaiyi
Stewart, Grant S.
Elledge, Stephen J.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2004-04-19
Volume: 101
Issue: 17
Pages: 6484-6489
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0401847101
PMC: PMC404071
OpenAlex: W2129258256
Cited by: 156
References: 27
Citations by year: 2026: 1 · 2025: 4 · 2024: 11 · 2023: 5 · 2022: 4 · 2021: 4 · 2020: 8 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 7
FWCI: 5.33
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Funders: Howard Hughes Medical Institute
National Institutes of Health
National Cancer Institute (F32CA093043)
National Institute of General Medical Sciences (GM-44664, R37GM044664, R01GM044664)
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 › Genetics › BRCA gene mutations in cancer
Keywords: Claspin, BRCA1, Chk1, ATR pathway, DNA damage response, genotoxic stress resistance, replication stress, cell proliferation, tumor suppressor, oncogenes, protein phosphorylation, hydroxyurea
MeSH terms: Base Sequence, Carrier Proteins, Cell Division, Cell Survival, DNA Damage, Humans, Oligoribonucleotides, Phosphorylation, Protein Binding, BRCA1 Protein, Xenopus Proteins, Adaptor Proteins, Signal Transducing

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.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks