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  • 1
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    Rapid destruction of human Cdc25A in response to DNA damage (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: To protect genome integrity and ensure survival, eukaryotic cells exposed to genotoxic stress cease proliferating to provide time for DNA repair. Human cells responded to ultraviolet light or ionizing radiation by rapid, ubiquitin- and proteasome-dependent protein degradation of Cdc25A, a phosphatase that is required for progression from G1 to S phase of the cell cycle. This response involved activated Chk1 protein kinase but not the p53 pathway, and the persisting inhibitory tyrosine phosphorylation of Cdk2 blocked entry into S phase and DNA replication. Overexpression of Cdc25A bypassed this mechanism, leading to enhanced DNA damage and decreased cell survival. These results identify specific degradation of Cdc25A as part of the DNA damage checkpoint mechanism and suggest how Cdc25A overexpression in human cancers might contribute to tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mailand, N -- Falck, J -- Lukas, C -- Syljuasen, R G -- Welcker, M -- Bartek, J -- Lukas, J -- New York, N.Y. -- Science. 2000 May 26;288(5470):1425-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Biology, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827953" target="_blank"〉PubMed〈/a〉
    Keywords: *CDC2-CDC28 Kinases ; Cell Line ; Cell Survival ; Cyclin E/metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Cysteine Endopeptidases/metabolism ; *DNA Damage ; DNA Repair ; DNA Replication ; G1 Phase ; Humans ; Multienzyme Complexes/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proteasome Endopeptidase Complex ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Recombinant Fusion Proteins/metabolism ; S Phase ; Transfection ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays ; cdc25 Phosphatases/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-02
    Description: DNA interstrand cross-links (ICLs) block replication fork progression by inhibiting DNA strand separation. Repair of ICLs requires sequential incisions, translesion DNA synthesis, and homologous recombination, but the full set of factors involved in these transactions remains unknown. We devised a technique called chromatin mass spectrometry (CHROMASS) to study protein recruitment dynamics during perturbed DNA replication in Xenopus egg extracts. Using CHROMASS, we systematically monitored protein assembly and disassembly on ICL-containing chromatin. Among numerous prospective DNA repair factors, we identified SLF1 and SLF2, which form a complex with RAD18 and together define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions. Our study provides a global analysis of an entire DNA repair pathway and reveals the mechanism of SMC5/6 relocalization to damaged DNA in vertebrate cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raschle, Markus -- Smeenk, Godelieve -- Hansen, Rebecca K -- Temu, Tikira -- Oka, Yasuyoshi -- Hein, Marco Y -- Nagaraj, Nagarjuna -- Long, David T -- Walter, Johannes C -- Hofmann, Kay -- Storchova, Zuzana -- Cox, Jurgen -- Bekker-Jensen, Simon -- Mailand, Niels -- Mann, Matthias -- HL098316/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2015 May 1;348(6234):1253671. doi: 10.1126/science.1253671. Epub 2015 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. ; Ubiquitin Signaling Group, Department of Disease Biology, Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, DK-2200 Copenhagen, Denmark. ; Howard Hughes Medical Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. ; Institute of Genetics, University of Cologne, 50674 Cologne, Germany. ; Maintenance of Genome Stability Group, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. ; Ubiquitin Signaling Group, Department of Disease Biology, Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, DK-2200 Copenhagen, Denmark. simon.bekker-jensen@cpr.ku.dk niels.mailand@cpr.ku.dk mmann@biochem.mpg.de. ; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. Novo Nordisk Foundation Center for Protein Research, Proteomics Program, University of Copenhagen, DK-2200 Copenhagen, Denmark. simon.bekker-jensen@cpr.ku.dk niels.mailand@cpr.ku.dk mmann@biochem.mpg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25931565" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/chemistry/metabolism ; *DNA Damage ; *DNA Repair ; DNA Repair Enzymes/*metabolism ; *DNA Replication ; DNA-Binding Proteins/metabolism ; Mass Spectrometry/methods ; Proteomics/methods ; RNA-Binding Proteins/metabolism ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage (2015)
    Nature Publishing Group (NPG)
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    Publication Date: 2015-10-28
    Description: DNA double-strand breaks (DSBs) are highly cytotoxic DNA lesions that trigger non-proteolytic ubiquitylation of adjacent chromatin areas to generate binding sites for DNA repair factors. This depends on the sequential actions of the E3 ubiquitin ligases RNF8 and RNF168 (refs 1-6), and UBC13 (also known as UBE2N), an E2 ubiquitin-conjugating enzyme that specifically generates K63-linked ubiquitin chains. Whereas RNF168 is known to catalyse ubiquitylation of H2A-type histones, leading to the recruitment of repair factors such as 53BP1 (refs 8-10), the critical substrates of RNF8 and K63-linked ubiquitylation remain elusive. Here we elucidate how RNF8 and UBC13 promote recruitment of RNF168 and downstream factors to DSB sites in human cells. We establish that UBC13-dependent K63-linked ubiquitylation at DSB sites is predominantly mediated by RNF8 but not RNF168, and that H1-type linker histones, but not core histones, represent major chromatin-associated targets of this modification. The RNF168 module (UDM1) recognizing RNF8-generated ubiquitylations is a high-affinity reader of K63-ubiquitylated H1, mechanistically explaining the essential roles of RNF8 and UBC13 in recruiting RNF168 to DSBs. Consistently, reduced expression or chromatin association of linker histones impair accumulation of K63-linked ubiquitin conjugates and repair factors at DSB-flanking chromatin. These results identify histone H1 as a key target of RNF8-UBC13 in DSB signalling and expand the concept of the histone code by showing that posttranslational modifications of linker histones can serve as important marks for recognition by factors involved in genome stability maintenance, and possibly beyond.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thorslund, Tina -- Ripplinger, Anita -- Hoffmann, Saskia -- Wild, Thomas -- Uckelmann, Michael -- Villumsen, Bine -- Narita, Takeo -- Sixma, Titia K -- Choudhary, Chunaram -- Bekker-Jensen, Simon -- Mailand, Niels -- England -- Nature. 2015 Nov 19;527(7578):389-93. doi: 10.1038/nature15401. Epub 2015 Oct 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ubiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark. ; Proteomics Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark. ; Division of Biochemistry, Cancer Genomics Center, Netherlands Cancer Institute, 1066 CX Amsterdam, the Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26503038" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/metabolism ; DNA Breaks, Double-Stranded ; *DNA Damage ; DNA Repair ; DNA-Binding Proteins/metabolism ; Histones/chemistry/*metabolism ; Humans ; Lysine/metabolism ; Protein Structure, Tertiary ; *Signal Transduction ; Ubiquitin/*metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/chemistry/metabolism ; Ubiquitination
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    SUMOylation promotes protective responses to DNA-protein crosslinks (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈p〉DNA-protein crosslinks (DPCs) are highly cytotoxic lesions that obstruct essential DNA transactions and whose resolution is critical for cell and organismal fitness. However, the mechanisms by which cells respond to and overcome DPCs remain incompletely understood. Recent studies unveiled a dedicated DPC repair pathway in higher eukaryotes involving the SprT-type metalloprotease SPRTN/DVC1, which proteolytically processes DPCs during DNA replication in a ubiquitin-regulated manner. Here, we show that chemically induced and defined enzymatic DPCs trigger potent chromatin SUMOylation responses targeting the crosslinked proteins and associated factors. Consequently, inhibiting SUMOylation compromises DPC clearance and cellular fitness. We demonstrate that ACRC/GCNA family SprT proteases interact with SUMO and establish important physiological roles of 〈i〉Caenorhabditis elegans 〈/i〉GCNA-1 and SUMOylation in promoting germ cell and embryonic survival upon DPC formation. Our findings provide first global insights into signaling responses to DPCs and reveal an evolutionarily conserved function of SUMOylation in facilitating responses to these lesions in metazoans that may complement replication-coupled DPC resolution processes.〈/p〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
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  • 5
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    SUMOylation promotes protective responses to DNA-protein crosslinks (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉 〈p〉DNA-protein crosslinks (DPCs) can be proteolytically removed in a replication- and ubiquitin-dependent manner. Here, DPC formation is found to also trigger a protective, local chromatin SUMOylation response promoting clearance of crosslinks.〈/p〉 〈p〉 〈l type="unord"〉〈li〉〈p〉Comprehensive proteomic profiling of reveals dynamic formaldehyde-induced chromatin SUMOylation in human cells.〈/p〉〈/li〉 〈li〉〈p〉SUMOylation directly targets defined enzymatic DNMT1-DNA crosslinks.〈/p〉〈/li〉 〈li〉〈p〉SUMOylation of defined enzymatic DPCs is required for lesion clearance and cell fitness.〈/p〉〈/li〉 〈li〉〈p〉The SprT-family protease GCNA-1 protects against DPC toxicity in 〈i〉Caenorhabditis elegans〈/i〉 via SUMO.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
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  • 6
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    Regulation of G2/M events by Cdc25A through phosphorylation-dependent modulation of its stability (2002)
    EMBO Press
    Details
    Publication Date: 2002-11-01
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by EMBO Press on behalf of European Molecular Biology Organization.
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