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Article ; Online: Viral manipulation of DNA repair and cell cycle checkpoints.

Chaurushiya, Mira S / Weitzman, Matthew D

2009 Volume 8, Issue 9, Page(s) 1166–1176

Abstract: Recognition and repair of DNA damage is critical for maintaining genomic integrity and suppressing tumorigenesis. In eukaryotic cells, the sensing and repair of DNA damage are coordinated with cell cycle progression and checkpoints, in order to prevent ... ...

Abstract	Recognition and repair of DNA damage is critical for maintaining genomic integrity and suppressing tumorigenesis. In eukaryotic cells, the sensing and repair of DNA damage are coordinated with cell cycle progression and checkpoints, in order to prevent the propagation of damaged DNA. The carefully maintained cellular response to DNA damage is challenged by viruses, which produce a large amount of exogenous DNA during infection. Viruses also express proteins that perturb cellular DNA repair and cell cycle pathways, promoting tumorigenesis in their quest for cellular domination. This review presents an overview of strategies employed by viruses to manipulate DNA damage responses and cell cycle checkpoints as they commandeer the cell to maximize their own viral replication. Studies of viruses have identified key cellular regulators and revealed insights into molecular mechanisms governing DNA repair, cell cycle checkpoints, and transformation.
MeSH term(s)	Animals ; Cell Cycle ; DNA Damage ; DNA Repair ; Humans ; Neoplasms/genetics ; Neoplasms/virology ; Virus Diseases/metabolism ; Virus Diseases/pathology ; Virus Diseases/therapy ; Viruses/metabolism
Language	English
Publishing date	2009-05-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2009.04.016
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Article ; Online: Changing the ubiquitin landscape during viral manipulation of the DNA damage response.

Weitzman, Matthew D / Lilley, Caroline E / Chaurushiya, Mira S

FEBS letters

2011 Volume 585, Issue 18, Page(s) 2897–2906

Abstract: Viruses often induce signaling through the same cellular cascades that are activated by damage to the cellular genome. Signaling triggered by viral proteins or exogenous DNA delivered by viruses can be beneficial or detrimental to viral infection. ... ...

Abstract	Viruses often induce signaling through the same cellular cascades that are activated by damage to the cellular genome. Signaling triggered by viral proteins or exogenous DNA delivered by viruses can be beneficial or detrimental to viral infection. Viruses have therefore evolved to dissect the cellular DNA damage response pathway during infection, often marking key cellular regulators with ubiquitin to induce their degradation or change their function. Signaling controlled by ubiquitin or ubiquitin-like proteins has recently emerged as key regulator of the cellular DNA damage response. Situated at the interface between DNA damage signaling and the ubiquitin system, viruses can reveal key convergence points in this important cellular pathway. In this review, we examine how viruses harness the diversity of the cellular ubiquitin system to modulate the DNA damage signaling pathway. We discuss the implications of viral infiltration of this pathway for both the transcriptional program of the virus and for the cellular response to DNA damage.
MeSH term(s)	DNA Damage ; DNA Repair ; Host-Pathogen Interactions ; Humans ; Signal Transduction ; Ubiquitin/metabolism ; Viral Proteins/metabolism ; Viral Proteins/physiology ; Virus Diseases/genetics ; Virus Diseases/physiopathology ; Virus Diseases/virology ; Viruses/metabolism
Chemical Substances	Ubiquitin ; Viral Proteins
Language	English
Publishing date	2011-05-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2011.04.049
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Article ; Online: Genomes in conflict: maintaining genome integrity during virus infection.

Weitzman, Matthew D / Lilley, Caroline E / Chaurushiya, Mira S

Annual review of microbiology

2010 Volume 64, Page(s) 61–81

Abstract: The cellular surveillance network for sensing and repairing damaged DNA prevents an array of human diseases, and when compromised it can lead to genomic instability and cancer. The carefully maintained cellular response to DNA damage is challenged during ...

Abstract	The cellular surveillance network for sensing and repairing damaged DNA prevents an array of human diseases, and when compromised it can lead to genomic instability and cancer. The carefully maintained cellular response to DNA damage is challenged during viral infection, when foreign DNA is introduced into the cell. The battle between virus and host generates a genomic conflict. The host attempts to limit viral infection and protect its genome, while the virus deploys tactics to eliminate, evade, or exploit aspects of the cellular defense. Studying this conflict has revealed that the cellular DNA damage response machinery comprises part of the intrinsic cellular defense against viral infection. In this review we examine recent advances in this emerging field. We identify common themes used by viruses in their attempts to commandeer or circumvent the host cell's DNA repair machinery, and highlight potential outcomes of the conflict for both virus and host.
MeSH term(s)	Animals ; DNA Damage ; DNA Repair ; Genomic Instability ; Humans ; Models, Biological ; Neoplasms/genetics ; Neoplasms/virology ; Virus Diseases/pathology ; Viruses/pathogenicity
Language	English
Publishing date	2010
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	207931-8
ISSN	1545-3251 ; 0066-4227
ISSN (online)	1545-3251
ISSN	0066-4227
DOI	10.1146/annurev.micro.112408.134016
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Article: Chromatin at the intersection of viral infection and DNA damage.

Lilley, Caroline E / Chaurushiya, Mira S / Weitzman, Matthew D

Biochimica et biophysica acta

2009 Volume 1799, Issue 3-4, Page(s) 319–327

Abstract: During infection, viruses cause global disruption to nuclear architecture in their attempt to take over the cell. In turn, the host responds with various defenses, which include chromatin-mediated silencing of the viral genome and activation of DNA ... ...

Abstract	During infection, viruses cause global disruption to nuclear architecture in their attempt to take over the cell. In turn, the host responds with various defenses, which include chromatin-mediated silencing of the viral genome and activation of DNA damage signaling pathways. Dynamic exchanges at chromatin, and specific post-translational modifications on histones have recently emerged as master controllers of DNA damage signaling and repair. Studying viral control of chromatin modifications is identifying histones as important players in the battle between host and virus for control of cell cycle and gene expression. These studies are revealing new complexities of the virus-host interaction, uncovering the potential of chromatin as an anti-viral defense mechanism, and also providing unique insights into the role of chromatin in DNA repair.
MeSH term(s)	Animals ; Cell Cycle/genetics ; Chromatin/physiology ; DNA Damage/genetics ; Histones/metabolism ; Humans ; Virus Diseases/genetics ; Viruses/pathogenicity
Chemical Substances	Chromatin ; Histones
Language	English
Publishing date	2009-07-17
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2009.06.007
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Article ; Online: Intrinsic apoptosis shapes the tumor spectrum linked to inactivation of the deubiquitinase BAP1.

He, Meng / Chaurushiya, Mira S / Webster, Joshua D / Kummerfeld, Sarah / Reja, Rohit / Chaudhuri, Subhra / Chen, Ying-Jiun / Modrusan, Zora / Haley, Benjamin / Dugger, Debra L / Eastham-Anderson, Jeffrey / Lau, Shari / Dey, Anwesha / Caothien, Roger / Roose-Girma, Merone / Newton, Kim / Dixit, Vishva M

Science (New York, N.Y.)

2019 Volume 364, Issue 6437, Page(s) 283–285

Abstract: Malignancies arising from mutation of tumor suppressors have unexplained tissue proclivity. For example, ...

Abstract	Malignancies arising from mutation of tumor suppressors have unexplained tissue proclivity. For example,
MeSH term(s)	Animals ; Apoptosis/genetics ; Carcinogenesis/genetics ; Gene Expression Regulation, Neoplastic ; Gene Knock-In Techniques ; Germ-Line Mutation ; Histones ; Humans ; Melanocytes/metabolism ; Melanocytes/pathology ; Melanoma/genetics ; Melanoma/pathology ; Mesothelioma/genetics ; Mesothelioma/pathology ; Mice ; Mice, Mutant Strains ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism ; Polycomb Repressive Complex 1/metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Tumor Suppressor Proteins/genetics ; Ubiquitin Thiolesterase/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Uveal Neoplasms/genetics ; Uveal Neoplasms/pathology
Chemical Substances	BAP1 protein, human ; BAP1 protein, mouse ; Histones ; Mcl1 protein, mouse ; Myeloid Cell Leukemia Sequence 1 Protein ; Proto-Oncogene Proteins c-bcl-2 ; Tumor Suppressor Proteins ; Bcl2 protein, mouse (114100-40-2) ; Polycomb Repressive Complex 1 (EC 2.3.2.27) ; Rnf2 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2019-04-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aav4902
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Article ; Online: The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0.

Lilley, Caroline E / Chaurushiya, Mira S / Boutell, Chris / Everett, Roger D / Weitzman, Matthew D

PLoS pathogens

2011 Volume 7, Issue 6, Page(s) e1002084

Abstract: Cellular restriction factors responding to herpesvirus infection include the ND10 components PML, Sp100 and hDaxx. During the initial stages of HSV-1 infection, novel sub-nuclear structures containing these ND10 proteins form in association with incoming ...

Abstract	Cellular restriction factors responding to herpesvirus infection include the ND10 components PML, Sp100 and hDaxx. During the initial stages of HSV-1 infection, novel sub-nuclear structures containing these ND10 proteins form in association with incoming viral genomes. We report that several cellular DNA damage response proteins also relocate to sites associated with incoming viral genomes where they contribute to the cellular front line defense. We show that recruitment of DNA repair proteins to these sites is independent of ND10 components, and instead is coordinated by the cellular ubiquitin ligases RNF8 and RNF168. The viral protein ICP0 targets RNF8 and RNF168 for degradation, thereby preventing the deposition of repressive ubiquitin marks and counteracting this repair protein recruitment. This study highlights important parallels between recognition of cellular DNA damage and recognition of viral genomes, and adds RNF8 and RNF168 to the list of factors contributing to the intrinsic antiviral defense against herpesvirus infection.
MeSH term(s)	Animals ; Cells, Cultured ; Chlorocebus aethiops ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; DNA Repair Enzymes/physiology ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Genome, Viral/immunology ; Herpesvirus 1, Human/genetics ; Herpesvirus 1, Human/immunology ; Humans ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Immediate-Early Proteins/physiology ; Immune Evasion/genetics ; Immune Evasion/physiology ; Immunity, Innate/genetics ; Immunity, Innate/physiology ; Mice ; Mice, Knockout ; Models, Biological ; Protein Processing, Post-Translational ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitin-Protein Ligases/physiology ; Vero Cells ; Viruses/immunology
Chemical Substances	DNA-Binding Proteins ; Immediate-Early Proteins ; RNF8 protein, human ; RNF168 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Vmw110 protein, Human herpesvirus 1 (EC 2.3.2.27) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2011-06-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1002084
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Article ; Online: The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0.

Caroline E Lilley / Mira S Chaurushiya / Chris Boutell / Roger D Everett / Matthew D Weitzman

PLoS Pathogens, Vol 7, Iss 6, p e

2011 Volume 1002084

Abstract	Cellular restriction factors responding to herpesvirus infection include the ND10 components PML, Sp100 and hDaxx. During the initial stages of HSV-1 infection, novel sub-nuclear structures containing these ND10 proteins form in association with incoming viral genomes. We report that several cellular DNA damage response proteins also relocate to sites associated with incoming viral genomes where they contribute to the cellular front line defense. We show that recruitment of DNA repair proteins to these sites is independent of ND10 components, and instead is coordinated by the cellular ubiquitin ligases RNF8 and RNF168. The viral protein ICP0 targets RNF8 and RNF168 for degradation, thereby preventing the deposition of repressive ubiquitin marks and counteracting this repair protein recruitment. This study highlights important parallels between recognition of cellular DNA damage and recognition of viral genomes, and adds RNF8 and RNF168 to the list of factors contributing to the intrinsic antiviral defense against herpesvirus infection.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2011-06-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article: Changing the ubiquitin landscape during viral manipulation of the DNA damage response

Weitzman, Matthew D / Lilley, Caroline E / Chaurushiya, Mira S

FEBS letters. 2011 Sept. 16, v. 585, no. 18

2011

Abstract	Viruses often induce signaling through the same cellular cascades that are activated by damage to the cellular genome. Signaling triggered by viral proteins or exogenous DNA delivered by viruses can be beneficial or detrimental to viral infection. Viruses have therefore evolved to dissect the cellular DNA damage response pathway during infection, often marking key cellular regulators with ubiquitin to induce their degradation or change their function. Signaling controlled by ubiquitin or ubiquitin-like proteins has recently emerged as key regulator of the cellular DNA damage response. Situated at the interface between DNA damage signaling and the ubiquitin system, viruses can reveal key convergence points in this important cellular pathway. In this review, we examine how viruses harness the diversity of the cellular ubiquitin system to modulate the DNA damage signaling pathway. We discuss the implications of viral infiltration of this pathway for both the transcriptional program of the virus and for the cellular response to DNA damage.
Keywords	DNA ; DNA damage ; genome ; signal transduction ; transcription (genetics) ; ubiquitin ; viral proteins ; viruses
Language	English
Dates of publication	2011-0916
Size	p. 2897-2906.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2011.04.049
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Article ; Online: The tumor suppressor BAP1 cooperates with BRAFV600E to promote tumor formation in cutaneous melanoma.

Webster, Joshua D / Pham, Trang H / Wu, Xiumin / Hughes, Nicolas W / Li, Zhongwu / Totpal, Klara / Lee, Ho-June / Calses, Philamer C / Chaurushiya, Mira S / Stawiski, Eric W / Modrusan, Zora / Chang, Matthew T / Tran, Christopher / Lee, Wyne P / Chalasani, Sreedevi / Hung, Jeffrey / Sharma, Neeraj / Chan, Sara / Hotzel, Kathy /

Talevich, Eric / Shain, Alan / Xu, Mengshu / Lill, Jennie / Dixit, Vishva M / Bastian, Boris C / Dey, Anwesha

Pigment cell & melanoma research

2018 Volume 32, Issue 2, Page(s) 269–279

Abstract: The deubiquitinating enzyme BAP1 is mutated in a hereditary cancer syndrome with a high risk of mesothelioma and melanocytic tumors. Here, we show that Bap1 deletion in melanocytes cooperates with the constitutively active, oncogenic form of BRAF ( ... ...

Abstract	The deubiquitinating enzyme BAP1 is mutated in a hereditary cancer syndrome with a high risk of mesothelioma and melanocytic tumors. Here, we show that Bap1 deletion in melanocytes cooperates with the constitutively active, oncogenic form of BRAF (BRAF
MeSH term(s)	Animals ; Carcinogenesis/genetics ; Carcinogenesis/pathology ; Cell Line, Tumor ; Cell Proliferation ; DNA Damage ; Epithelial-Mesenchymal Transition/genetics ; Gene Deletion ; Gene Expression Regulation, Neoplastic ; Histones/metabolism ; Lung Neoplasms/genetics ; Lung Neoplasms/pathology ; Melanocytes/metabolism ; Melanocytes/pathology ; Melanoma/genetics ; Melanoma/pathology ; Mice, Inbred C57BL ; Mice, Knockout ; Mutation/genetics ; Proto-Oncogene Proteins B-raf/genetics ; Skin Neoplasms/genetics ; Skin Neoplasms/pathology ; Transcription, Genetic ; Tumor Suppressor Proteins/metabolism ; Ubiquitin Thiolesterase/metabolism ; Ubiquitination ; Melanoma, Cutaneous Malignant
Chemical Substances	BAP1 protein, mouse ; Histones ; Tumor Suppressor Proteins ; Proto-Oncogene Proteins B-raf (EC 2.7.11.1) ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2018-09-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2409570-9
ISSN	1755-148X ; 1600-0749 ; 0893-5785 ; 1755-1471
ISSN (online)	1755-148X ; 1600-0749
ISSN	0893-5785 ; 1755-1471
DOI	10.1111/pcmr.12735
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Article ; Online: Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain.

Chaurushiya, Mira S / Lilley, Caroline E / Aslanian, Aaron / Meisenhelder, Jill / Scott, Daniel C / Landry, Sébastien / Ticau, Simina / Boutell, Chris / Yates, John R / Schulman, Brenda A / Hunter, Tony / Weitzman, Matthew D

Molecular cell

2012 Volume 46, Issue 1, Page(s) 79–90

Abstract: Viral hijacking of cellular processes relies on the ability to mimic the structure or function of cellular proteins. Many viruses encode ubiquitin ligases to facilitate infection, although the mechanisms by which they select their substrates are often ... ...

Abstract	Viral hijacking of cellular processes relies on the ability to mimic the structure or function of cellular proteins. Many viruses encode ubiquitin ligases to facilitate infection, although the mechanisms by which they select their substrates are often unknown. The Herpes Simplex Virus type-1-encoded E3 ubiquitin ligase, ICP0, promotes infection through degradation of cellular proteins, including the DNA damage response E3 ligases RNF8 and RNF168. Here we describe a mechanism by which this viral E3 hijacks a cellular phosphorylation-based targeting strategy to degrade RNF8. By mimicking a cellular phosphosite, ICP0 binds RNF8 via the RNF8 forkhead associated (FHA) domain. Phosphorylation of ICP0 T67 by CK1 recruits RNF8 for degradation and thereby promotes viral transcription, replication, and progeny production. We demonstrate that this mechanism may constitute a broader viral strategy to target other cellular factors, highlighting the importance of this region of the ICP0 protein in countering intrinsic antiviral defenses.
MeSH term(s)	Animals ; Chlorocebus aethiops ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Herpesvirus 1, Human/physiology ; Humans ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Molecular Mimicry/physiology ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Proteolysis ; Transcription, Genetic/physiology ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Vero Cells ; Virus Replication/physiology
Chemical Substances	DNA-Binding Proteins ; Immediate-Early Proteins ; RNF8 protein, human ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Vmw110 protein, Human herpesvirus 1 (EC 2.3.2.27)
Language	English
Publishing date	2012-03-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2012.02.004
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