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Article ; Online: PARP1, DIDO3, and DHX9 Proteins Mutually Interact in Mouse Fibroblasts, with Effects on DNA Replication Dynamics, Senescence, and Oncogenic Transformation.

Fütterer, Agnes / Rodriguez-Acebes, Sara / Méndez, Juan / Gutiérrez, Julio / Martínez-A, Carlos

2024 Volume 13, Issue 2

Abstract: The regulated formation and resolution of R-loops is a natural process in physiological gene expression. Defects in R-loop metabolism can lead to DNA replication stress, which is associated with a variety of diseases and, ultimately, with cancer. The ... ...

Abstract	The regulated formation and resolution of R-loops is a natural process in physiological gene expression. Defects in R-loop metabolism can lead to DNA replication stress, which is associated with a variety of diseases and, ultimately, with cancer. The proteins PARP1, DIDO3, and DHX9 are important players in R-loop regulation. We previously described the interaction between DIDO3 and DHX9. Here, we show that, in mouse embryonic fibroblasts, the three proteins are physically linked and dependent on PARP1 activity. The C-terminal truncation of DIDO3 leads to the impairment of this interaction; concomitantly, the cells show increased replication stress and senescence. DIDO3 truncation also renders the cells partially resistant to in vitro oncogenic transformation, an effect that can be reversed by immortalization. We propose that PARP1, DIDO3, and DHX9 proteins form a ternary complex that regulates R-loop metabolism, preventing DNA replication stress and subsequent senescence.
MeSH term(s)	Animals ; Mice ; DNA Replication ; Fibroblasts ; Poly (ADP-Ribose) Polymerase-1/metabolism ; Poly (ADP-Ribose) Polymerase-1/physiology ; DEAD-box RNA Helicases/metabolism ; DEAD-box RNA Helicases/physiology ; Cellular Senescence/genetics ; Carcinogenesis/genetics
Chemical Substances	Parp1 protein, mouse (EC 2.4.2.30) ; Poly (ADP-Ribose) Polymerase-1 (EC 2.4.2.30) ; Dido protein, mouse ; Dhx9 protein, mouse ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2024-01-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13020159
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Article ; Online: RAD51 restricts DNA over-replication from re-activated origins.

Muñoz, Sergio / Blanco-Romero, Elena / González-Acosta, Daniel / Rodriguez-Acebes, Sara / Megías, Diego / Lopes, Massimo / Méndez, Juan

The EMBO journal

2024 Volume 43, Issue 6, Page(s) 1043–1064

Abstract: Eukaryotic cells rely on several mechanisms to ensure that the genome is duplicated precisely once in each cell division cycle, preventing DNA over-replication and genomic instability. Most of these mechanisms limit the activity of origin licensing ... ...

Abstract	Eukaryotic cells rely on several mechanisms to ensure that the genome is duplicated precisely once in each cell division cycle, preventing DNA over-replication and genomic instability. Most of these mechanisms limit the activity of origin licensing proteins to prevent the reactivation of origins that have already been used. Here, we have investigated whether additional controls restrict the extension of re-replicated DNA in the event of origin re-activation. In a genetic screening in cells forced to re-activate origins, we found that re-replication is limited by RAD51 and enhanced by FBH1, a RAD51 antagonist. In the presence of chromatin-bound RAD51, forks stemming from re-fired origins are slowed down, leading to frequent events of fork reversal. Eventual re-initiation of DNA synthesis mediated by PRIMPOL creates ssDNA gaps that facilitate the partial elimination of re-duplicated DNA by MRE11 exonuclease. In the absence of RAD51, these controls are abrogated and re-replication forks progress much longer than in normal conditions. Our study uncovers a safeguard mechanism to protect genome stability in the event of origin reactivation.
MeSH term(s)	DNA/genetics ; DNA Replication ; DNA-Binding Proteins/metabolism ; MRE11 Homologue Protein/metabolism ; Rad51 Recombinase/genetics ; Rad51 Recombinase/metabolism ; Humans
Chemical Substances	DNA (9007-49-2) ; DNA-Binding Proteins ; MRE11 Homologue Protein (EC 3.1.-) ; Rad51 Recombinase (EC 2.7.7.-) ; RAD51 protein, human (EC 2.7.7.-)
Language	English
Publishing date	2024-02-15
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/s44318-024-00038-z
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Uncoupling fork speed and origin activity to identify the primary cause of replicative stress phenotypes.

Rodriguez-Acebes, Sara / Mourón, Silvana / Méndez, Juan

The Journal of biological chemistry

2018 Volume 293, Issue 33, Page(s) 12855–12861

Abstract: In growing cells, DNA replication precedes mitotic cell division to transmit genetic information to the next generation. The slowing or stalling of DNA replication forks at natural or exogenous obstacles causes "replicative stress" that promotes genomic ... ...

Abstract	In growing cells, DNA replication precedes mitotic cell division to transmit genetic information to the next generation. The slowing or stalling of DNA replication forks at natural or exogenous obstacles causes "replicative stress" that promotes genomic instability and affects cellular fitness. Replicative stress phenotypes can be characterized at the single-molecule level with DNA combing or stretched DNA fibers, but interpreting the results obtained with these approaches is complicated by the fact that the speed of replication forks is connected to the frequency of origin activation. Primary alterations in fork speed trigger secondary responses in origins, and, conversely, primary alterations in the number of active origins induce compensatory changes in fork speed. Here, by employing interventions that temporally restrict either fork speed or origin firing while still allowing interrogation of the other variable, we report a set of experimental conditions to separate cause and effect in any manipulation that affects DNA replication dynamics. Using HeLa cells and chemical inhibition of origin activity (through a CDC7 kinase inhibitor) and of DNA synthesis (via the DNA polymerase inhibitor aphidicolin), we found that primary effects of replicative stress on velocity of replisomes (fork rate) can be readily distinguished from primary effects on origin firing. Identifying the primary cause of replicative stress in each case as demonstrated here may facilitate the design of methods to counteract replication stress in primary cells or to enhance it in cancer cells to increase their susceptibility to therapies that target DNA repair.
MeSH term(s)	Aphidicolin/pharmacology ; Cell Cycle Proteins/antagonists & inhibitors ; Cell Cycle Proteins/metabolism ; Cellular Senescence/drug effects ; DNA/biosynthesis ; DNA Repair/drug effects ; DNA Replication/drug effects ; HeLa Cells ; Humans ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/metabolism ; Replication Origin
Chemical Substances	Cell Cycle Proteins ; Aphidicolin (38966-21-1) ; DNA (9007-49-2) ; CDC7 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2018-06-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.003740
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Article ; Online: Regulation of Claspin by the p38 stress-activated protein kinase protects cells from DNA damage.

Ulsamer, Arnau / Martínez-Limón, Adrián / Bader, Sina / Rodríguez-Acebes, Sara / Freire, Raimundo / Méndez, Juan / de Nadal, Eulàlia / Posas, Francesc

Cell reports

2022 Volume 40, Issue 12, Page(s) 111375

Abstract: Stress-activated protein kinases (SAPKs) enhance survival in response to environmental changes. In yeast, the Hog1 SAPK and Mrc1, a protein required for DNA replication, define a safeguard mechanism that allows eukaryotic cells to prevent genomic ... ...

Abstract	Stress-activated protein kinases (SAPKs) enhance survival in response to environmental changes. In yeast, the Hog1 SAPK and Mrc1, a protein required for DNA replication, define a safeguard mechanism that allows eukaryotic cells to prevent genomic instability upon stress during S-phase. Here we show that, in mammals, the p38 SAPK and Claspin-the functional homolog of Mrc1-protect cells from DNA damage upon osmostress during S-phase. We demonstrate that p38 phosphorylates Claspin and either the mutation of the p38-phosphorylation sites in Claspin or p38 inhibition suppresses the protective role of Claspin on DNA damage. In addition, wild-type Claspin but not the p38-unphosphorylatable mutant has a protective effect on cell survival in response to cisplatin treatment. These findings reveal a role of Claspin in response to chemotherapeutic drugs. Thus, this pathway protects S-phase integrity from different insults and it is conserved from yeast to mammals.
MeSH term(s)	Adaptor Proteins, Signal Transducing ; Animals ; Cell Cycle Proteins/metabolism ; Cisplatin/pharmacology ; DNA Damage ; DNA Replication ; Mammals/metabolism ; Protein Serine-Threonine Kinases ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Cisplatin (Q20Q21Q62J)
Language	English
Publishing date	2022-09-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111375
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Article ; Online: RHOJ controls EMT-associated resistance to chemotherapy.

Debaugnies, Maud / Rodríguez-Acebes, Sara / Blondeau, Jeremy / Parent, Marie-Astrid / Zocco, Manuel / Song, Yura / de Maertelaer, Viviane / Moers, Virginie / Latil, Mathilde / Dubois, Christine / Coulonval, Katia / Impens, Francis / Van Haver, Delphi / Dufour, Sara / Uemura, Akiyoshi / Sotiropoulou, Panagiota A / Méndez, Juan / Blanpain, Cédric

Nature

2023 Volume 616, Issue 7955, Page(s) 168–175

Abstract: The resistance of cancer cells to therapy is responsible for the death of most patients with ... ...

Abstract	The resistance of cancer cells to therapy is responsible for the death of most patients with cancer
MeSH term(s)	Actins/drug effects ; Actins/metabolism ; Carcinoma, Squamous Cell/drug therapy ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Line, Tumor ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Epithelial-Mesenchymal Transition/drug effects ; Proteomics ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism ; Animals ; Mice ; Skin Neoplasms/drug therapy ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; Gene Expression Profiling ; Genome
Chemical Substances	Actins ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Rhoj protein, mouse
Language	English
Publishing date	2023-03-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-05838-7
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: 3D chromatin connectivity underlies replication origin efficiency in mouse embryonic stem cells.

Jodkowska, Karolina / Pancaldi, Vera / Rigau, Maria / Almeida, Ricardo / Fernández-Justel, José M / Graña-Castro, Osvaldo / Rodríguez-Acebes, Sara / Rubio-Camarillo, Miriam / Carrillo-de Santa Pau, Enrique / Pisano, David / Al-Shahrour, Fátima / Valencia, Alfonso / Gómez, María / Méndez, Juan

Nucleic acids research

2022

Abstract: In mammalian cells, chromosomal replication starts at thousands of origins at which replisomes are assembled. Replicative stress triggers additional initiation events from 'dormant' origins whose genomic distribution and regulation are not well ... ...

Abstract	In mammalian cells, chromosomal replication starts at thousands of origins at which replisomes are assembled. Replicative stress triggers additional initiation events from 'dormant' origins whose genomic distribution and regulation are not well understood. In this study, we have analyzed origin activity in mouse embryonic stem cells in the absence or presence of mild replicative stress induced by aphidicolin, a DNA polymerase inhibitor, or by deregulation of origin licensing factor CDC6. In both cases, we observe that the majority of stress-responsive origins are also active in a small fraction of the cell population in a normal S phase, and stress increases their frequency of activation. In a search for the molecular determinants of origin efficiency, we compared the genetic and epigenetic features of origins displaying different levels of activation, and integrated their genomic positions in three-dimensional chromatin interaction networks derived from high-depth Hi-C and promoter-capture Hi-C data. We report that origin efficiency is directly proportional to the proximity to transcriptional start sites and to the number of contacts established between origin-containing chromatin fragments, supporting the organization of origins in higher-level DNA replication factories.
Language	English
Publishing date	2022-12-01
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkac1111
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Article ; Online: In Vivo DNA Re-replication Elicits Lethal Tissue Dysplasias.

Muñoz, Sergio / Búa, Sabela / Rodríguez-Acebes, Sara / Megías, Diego / Ortega, Sagrario / de Martino, Alba / Méndez, Juan

Cell reports

2017 Volume 19, Issue 5, Page(s) 928–938

Abstract: Mammalian DNA replication origins are "licensed" by the loading of DNA helicases, a reaction that is mediated by CDC6 and CDT1 proteins. After initiation of DNA synthesis, CDC6 and CDT1 are inhibited to prevent origin reactivation and DNA overreplication ...

Abstract	Mammalian DNA replication origins are "licensed" by the loading of DNA helicases, a reaction that is mediated by CDC6 and CDT1 proteins. After initiation of DNA synthesis, CDC6 and CDT1 are inhibited to prevent origin reactivation and DNA overreplication before cell division. CDC6 and CDT1 are highly expressed in many types of cancer cells, but the impact of their deregulated expression had not been investigated in vivo. Here, we have generated mice strains that allow the conditional overexpression of both proteins. Adult mice were unharmed by the individual overexpression of either CDC6 or CDT1, but their combined deregulation led to DNA re-replication in progenitor cells and lethal tissue dysplasias. This study offers mechanistic insights into the necessary cooperation between CDC6 and CDT1 for facilitation of origin reactivation and describes the physiological consequences of DNA overreplication.
Language	English
Publishing date	2017-05-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2017.04.032
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Article ; Online: PDS5 proteins are required for proper cohesin dynamics and participate in replication fork protection.

Morales, Carmen / Ruiz-Torres, Miguel / Rodríguez-Acebes, Sara / Lafarga, Vanesa / Rodríguez-Corsino, Miriam / Megías, Diego / Cisneros, David A / Peters, Jan-Michael / Méndez, Juan / Losada, Ana

The Journal of biological chemistry

2019 Volume 295, Issue 1, Page(s) 146–157

Abstract: Cohesin is a chromatin-bound complex that mediates sister chromatid cohesion and facilitates long-range interactions through DNA looping. How the transcription and replication machineries deal with the presence of cohesin on chromatin remains unclear. ... ...

Abstract	Cohesin is a chromatin-bound complex that mediates sister chromatid cohesion and facilitates long-range interactions through DNA looping. How the transcription and replication machineries deal with the presence of cohesin on chromatin remains unclear. The dynamic association of cohesin with chromatin depends on WAPL cohesin release factor (WAPL) and on PDS5 cohesin-associated factor (PDS5), which exists in two versions in vertebrate cells, PDS5A and PDS5B. Using genetic deletion in mouse embryo fibroblasts and a combination of CRISPR-mediated gene editing and RNAi-mediated gene silencing in human cells, here we analyzed the consequences of PDS5 depletion for DNA replication. We found that either PDS5A or PDS5B is sufficient for proper cohesin dynamics and that their simultaneous removal increases cohesin's residence time on chromatin and slows down DNA replication. A similar phenotype was observed in WAPL-depleted cells. Cohesin down-regulation restored normal replication fork rates in PDS5-deficient cells, suggesting that chromatin-bound cohesin hinders the advance of the replisome. We further show that PDS5 proteins are required to recruit WRN helicase-interacting protein 1 (WRNIP1), RAD51 recombinase (RAD51), and BRCA2 DNA repair associated (BRCA2) to stalled forks and that in their absence, nascent DNA strands at unprotected forks are degraded by MRE11 homolog double-strand break repair nuclease (MRE11). These findings indicate that PDS5 proteins participate in replication fork protection and also provide insights into how cohesin and its regulators contribute to the response to replication stress, a common feature of cancer cells.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities/metabolism ; Animals ; BRCA2 Protein/metabolism ; Cell Cycle Proteins/metabolism ; Cells, Cultured ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; DNA Replication ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Humans ; MRE11 Homologue Protein/metabolism ; Mice ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Rad51 Recombinase/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Cohesins
Chemical Substances	BRCA2 Protein ; BRCA2 protein, human ; Cell Cycle Proteins ; Chromatin ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Mre11a protein, mouse ; Nuclear Proteins ; PDS5A protein, human ; PDS5B protein, human ; Transcription Factors ; RAD51 protein, human (EC 2.7.7.-) ; Rad51 Recombinase (EC 2.7.7.-) ; MRE11 Homologue Protein (EC 3.1.-) ; WRNIP1 protein, human (EC 3.6.1.3) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-)
Language	English
Publishing date	2019-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.011099
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Article ; Online: USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication.

Hernández-Pérez, Santiago / Cabrera, Elisa / Amoedo, Hugo / Rodríguez-Acebes, Sara / Koundrioukoff, Stephane / Debatisse, Michelle / Méndez, Juan / Freire, Raimundo

Molecular oncology

2016 Volume 10, Issue 8, Page(s) 1196–1206

Abstract: DNA replication control is a key process in maintaining genomic integrity. Monitoring DNA replication initiation is particularly important as it needs to be coordinated with other cellular events and should occur only once per cell cycle. Crucial players ...

Abstract	DNA replication control is a key process in maintaining genomic integrity. Monitoring DNA replication initiation is particularly important as it needs to be coordinated with other cellular events and should occur only once per cell cycle. Crucial players in the initiation of DNA replication are the ORC protein complex, marking the origin of replication, and the Cdt1 and Cdc6 proteins, that license these origins to replicate by recruiting the MCM2-7 helicase. To accurately achieve its functions, Cdt1 is tightly regulated. Cdt1 levels are high from metaphase and during G1 and low in S/G2 phases of the cell cycle. This control is achieved, among other processes, by ubiquitination and proteasomal degradation. In an overexpression screen for Cdt1 deubiquitinating enzymes, we isolated USP37, to date the first ubiquitin hydrolase controlling Cdt1. USP37 overexpression stabilizes Cdt1, most likely a phosphorylated form of the protein. In contrast, USP37 knock down destabilizes Cdt1, predominantly during G1 and G1/S phases of the cell cycle. USP37 interacts with Cdt1 and is able to de-ubiquitinate Cdt1 in vivo and, USP37 is able to regulate the loading of MCM complexes onto the chromatin. In addition, downregulation of USP37 reduces DNA replication fork speed. Taken together, here we show that the deubiquitinase USP37 plays an important role in the regulation of DNA replication. Whether this is achieved via Cdt1, a central protein in this process, which we have shown to be stabilized by USP37, or via additional factors, remains to be tested.
MeSH term(s)	Cell Cycle Proteins/metabolism ; Cell Line ; DNA Replication ; Endopeptidases/metabolism ; G1 Phase ; Humans ; Phosphorylation ; Protein Binding ; S Phase ; Ubiquitination
Chemical Substances	CDT1 protein, human ; Cell Cycle Proteins ; Endopeptidases (EC 3.4.-) ; USP37 protein, human (EC 3.4.99.-)
Language	English
Publishing date	2016-06-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	2415106-3
ISSN	1878-0261 ; 1574-7891
ISSN (online)	1878-0261
ISSN	1574-7891
DOI	10.1016/j.molonc.2016.05.008
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Article ; Online: TIAR marks nuclear G2/M transition granules and restricts CDK1 activity under replication stress.

Lafarga, Vanesa / Sung, Hsu-Min / Haneke, Katharina / Roessig, Lea / Pauleau, Anne-Laure / Bruer, Marius / Rodriguez-Acebes, Sara / Lopez-Contreras, Andres J / Gruss, Oliver J / Erhardt, Sylvia / Mendez, Juan / Fernandez-Capetillo, Oscar / Stoecklin, Georg

EMBO reports

2018 Volume 20, Issue 1

Abstract: The G2/M checkpoint coordinates DNA replication with mitosis and thereby prevents chromosome segregation in the presence of unreplicated or damaged DNA Here, we show that the RNA-binding protein TIAR is essential for the G2/M checkpoint and that TIAR ... ...

Abstract	The G2/M checkpoint coordinates DNA replication with mitosis and thereby prevents chromosome segregation in the presence of unreplicated or damaged DNA Here, we show that the RNA-binding protein TIAR is essential for the G2/M checkpoint and that TIAR accumulates in nuclear foci in late G2 and prophase in cells suffering from replication stress. These foci, which we named G2/M transition granules (GMGs), occur at low levels in normally cycling cells and are strongly induced by replication stress. In addition to replication stress response proteins, GMGs contain factors involved in RNA metabolism as well as CDK1. Depletion of TIAR accelerates mitotic entry and leads to chromosomal instability in response to replication stress, in a manner that can be alleviated by the concomitant depletion of Cdc25B or inhibition of CDK1. Since TIAR retains CDK1 in GMGs and attenuates CDK1 activity, we propose that the assembly of GMGs may represent a so far unrecognized mechanism that contributes to the activation of the G2/M checkpoint in mammalian cells.
MeSH term(s)	CDC2 Protein Kinase/genetics ; Cell Cycle/genetics ; Chromosome Segregation/genetics ; DNA Damage/genetics ; DNA Replication/genetics ; G2 Phase Cell Cycle Checkpoints/genetics ; HeLa Cells ; Humans ; Mitosis/genetics ; Phosphorylation ; RNA-Binding Proteins/genetics ; cdc25 Phosphatases/genetics
Chemical Substances	RNA-Binding Proteins ; TIAL1 protein, human (148592-68-1) ; CDC2 Protein Kinase (EC 2.7.11.22) ; CDK1 protein, human (EC 2.7.11.22) ; CDC25B protein, human (EC 3.1.3.48) ; cdc25 Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2018-12-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201846224
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