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Pirh2 E3 Ubiquitin Ligase Monoubiquitinates DNA Polymerase Eta To Suppress Translesion DNA Synthesis

https://doi.org/10.1128/mcb.05808-11
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s11033-010-0099-xopenalex-snapshot
Interplay between MDM2, MDMX, Pirh2 and COP1: the negative regulators of p53
inferredcites →https://doi.org/10.1016/j.cell.2006.02.020openalex-snapshot
Crystal Structure of the Ubiquitin Binding Domains of Rabex-5 Reveals Two Modes of Interaction with Ubiquitin
inferredcites →https://doi.org/10.1016/j.cell.2007.05.044openalex-snapshot
Regulation of Pax3 by Proteasomal Degradation of Monoubiquitinated Protein in Skeletal Muscle Progenitors
inferredcites →https://doi.org/10.1016/j.molcel.2009.12.039openalex-snapshot
Regulation of Translesion Synthesis DNA Polymerase η by Monoubiquitination
inferredcites →https://doi.org/10.1016/j.molcel.2010.05.001openalex-snapshot
Monoubiquitination of RPN10 Regulates Substrate Recruitment to the Proteasome
inferredcites →https://doi.org/10.1016/s0092-8674(03)00193-4openalex-snapshot
Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation
inferredcites →https://doi.org/10.1016/s1097-2765(04)00259-xopenalex-snapshot
Interaction of Human DNA Polymerase η with Monoubiquitinated PCNA
inferredcites →https://doi.org/10.1038/21447openalex-snapshot
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
inferredcites →https://doi.org/10.1038/35077232openalex-snapshot
Genome maintenance mechanisms for preventing cancer
inferredcites →https://doi.org/10.1038/nature00991openalex-snapshot
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
inferredcites →https://doi.org/10.1038/ncb1436openalex-snapshot
Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
inferredcites →https://doi.org/10.1038/nrg2663openalex-snapshot
Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity
inferredcites →https://doi.org/10.1038/nrm1701openalex-snapshot
Ubiquitin-binding domains
inferredcites →https://doi.org/10.1038/nsmb.1521openalex-snapshot
Molecular basis of Pirh2-mediated p53 ubiquitylation
inferredcites →https://doi.org/10.1038/sj.emboj.7601178openalex-snapshot
Controlling the subcellular localization of DNA polymerases ι and η via interactions with ubiquitin
inferredcites →https://doi.org/10.1073/pnas.0808589105openalex-snapshot
Human DNA polymerase η activity and translocation is regulated by phosphorylation
inferredcites →https://doi.org/10.1074/jbc.270.29.17442openalex-snapshot
A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal
inferredcites →https://doi.org/10.1074/jbc.m312712200openalex-snapshot
Control of Human PIRH2 Protein Stability
inferredcites →https://doi.org/10.1074/jbc.m707722200openalex-snapshot
Physical Interactions and Functional Coupling between Daxx and Sodium Hydrogen Exchanger 1 in Ischemic Cell Death
inferredcites →https://doi.org/10.1093/jnci/djh292openalex-snapshot
Expression of Pirh2, a Newly Identified Ubiquitin Protein Ligase, in Lung Cancer
inferredcites →https://doi.org/10.1111/j.1349-7006.2009.01122.xopenalex-snapshot
High expression of Pirh2, an E3 ligase for p27, is associated with low expression of p27 and poor prognosis in head and neck cancers
inferredcites →https://doi.org/10.1126/science.1070236openalex-snapshot
Specialized DNA Polymerases, Cellular Survival, and the Genesis of Mutations
inferredcites →https://doi.org/10.1126/science.1120615openalex-snapshot
Ubiquitin-Binding Domains in Y-Family Polymerases Regulate Translesion Synthesis
inferredcites →https://doi.org/10.1126/science.285.5425.263openalex-snapshot
hRAD30 Mutations in the Variant Form of Xeroderma Pigmentosum
inferredcites →https://doi.org/10.1128/mcb.00147-06openalex-snapshot
Human PIRH2 Enhances Androgen Receptor Signaling through Inhibition of Histone Deacetylase 1 and Is Overexpressed in Prostate Cancer
inferredcites →https://doi.org/10.1128/mcb.01198-09openalex-snapshot
Pirh2 E3 Ubiquitin Ligase Targets DNA Polymerase Eta for 20S Proteasomal Degradation
inferredcites →https://doi.org/10.1128/mcb.01824-08openalex-snapshot
Masking of a Nuclear Signal Motif by Monoubiquitination Leads to Mislocalization and Degradation of the Regulatory Enzyme Cytidylyltransferase
inferredcites →https://doi.org/10.1128/mcb.26.4.1398-1413.2006openalex-snapshot
DNA Polymerase η, the Product of the Xeroderma Pigmentosum Variant Gene and a Target of p53, Modulates the DNA Damage Checkpoint and p53 Activation
inferredcites →https://doi.org/10.1146/annurev.biochem.74.082803.133250openalex-snapshot
EUKARYOTIC TRANSLESION SYNTHESIS DNA POLYMERASES: Specificity of Structure and Function

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.3185110openalex-extracted
Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis and Cancer Etiology
inferred← citeshttps://doi.org/10.1002/em.22359openalex-snapshot
Regulation of translesion DNA synthesis in mammalian cells
inferred← citeshttps://doi.org/10.1002/ijc.28129openalex-snapshot
A portrayal of E3 ubiquitin ligases and deubiquitylases in cancer
inferred← citeshttps://doi.org/10.1002/jcp.30155openalex-snapshot
DNA polymerase eta: A potential pharmacological target for cancer therapy
inferred← citeshttps://doi.org/10.1007/978-4-431-55873-6_11openalex-snapshot
Translesion DNA Synthesis and Damage Tolerance Pathways
inferred← citeshttps://doi.org/10.1007/978-981-10-6955-0_19openalex-snapshot
Regulation of Mammalian DNA Replication via the Ubiquitin-Proteasome System
inferred← citeshttps://doi.org/10.1007/s10555-017-9703-zopenalex-snapshot
E3 ubiquitin ligases in cancer and implications for therapies
inferred← citeshttps://doi.org/10.1016/b978-0-12-819460-7.00130-4openalex-snapshot
DNA repair | XPV Polymerase and the Bypass of Ultraviolet DNA Damage
inferred← citeshttps://doi.org/10.1016/j.bbrc.2012.10.135openalex-snapshot
Androgen receptor primes prostate cancer cells to apoptosis through down-regulation of basal p21 expression
inferred← citeshttps://doi.org/10.1016/j.canlet.2014.10.024openalex-snapshot
Enhanced anticancer activity of a protein phosphatase 2A inhibitor on chemotherapy and radiation in head and neck squamous cell carcinoma
inferred← citeshttps://doi.org/10.1016/j.dnarep.2015.02.011openalex-snapshot
Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins
inferred← citeshttps://doi.org/10.1016/j.dnarep.2015.02.017openalex-snapshot
Aberrant C-terminal domain of polymerase η targets the functional enzyme to the proteosomal degradation pathway
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.03.052openalex-snapshot
Pirh2 RING‐finger E3 ubiquitin ligase: Its role in tumorigenesis and cancer therapy
inferred← citeshttps://doi.org/10.1016/j.isci.2018.07.009openalex-snapshot
Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis
inferred← citeshttps://doi.org/10.1016/j.mrrev.2022.108436openalex-snapshot
Current state of knowledge of human DNA polymerase eta protein structure and disease-causing mutations
inferred← citeshttps://doi.org/10.1016/j.yexcr.2014.07.009openalex-snapshot
Tolerating DNA damage during eukaryotic chromosome replication
inferred← citeshttps://doi.org/10.1021/jacs.2c05312openalex-snapshot
Polymerase η Recruits DHX9 Helicase to Promote Replication across Guanine Quadruplex Structures
inferred← citeshttps://doi.org/10.1038/jid.2012.466openalex-snapshot
Pirh2 E3 Ubiquitin Ligase Modulates Keratinocyte Differentiation through p63
inferred← citeshttps://doi.org/10.1038/nrm3289openalex-snapshot
Y-family DNA polymerases and their role in tolerance of cellular DNA damage
inferred← citeshttps://doi.org/10.1038/onc.2013.494openalex-snapshot
FATS is an E2-independent ubiquitin ligase that stabilizes p53 and promotes its activation in response to DNA damage
inferred← citeshttps://doi.org/10.1038/s41467-017-02164-1openalex-snapshot
Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis
inferred← citeshttps://doi.org/10.1042/bj20141164openalex-snapshot
DNA polymerase η is regulated by poly(rC)-binding protein 1 via mRNA stability
inferred← citeshttps://doi.org/10.1074/jbc.ra120.013780openalex-snapshot
Multisite SUMOylation restrains DNA polymerase η interactions with DNA damage sites
inferred← citeshttps://doi.org/10.1080/10409238.2017.1291576openalex-snapshot
Translesion DNA polymerases in eukaryotes: what makes them tick?
inferred← citeshttps://doi.org/10.1093/nar/gkag098openalex-snapshot
Human DNA polymerase η is regulated by mutually exclusive mono-ubiquitination and mono-NEDDylation
inferred← citeshttps://doi.org/10.1093/nar/gkt016openalex-snapshot
A non-catalytic role of DNA polymerase η in recruiting Rad18 and promoting PCNA monoubiquitination at stalled replication forks
inferred← citeshttps://doi.org/10.1093/nar/gkx619openalex-snapshot
Phosphorylation regulates human polη stability and damage bypass throughout the cell cycle
inferred← citeshttps://doi.org/10.1099/jgv.0.001918openalex-snapshot
SARS-CoV-2 and the DNA damage response
inferred← citeshttps://doi.org/10.1101/2024.10.12.618026openalex-snapshot
DNA polymerase η is regulated by mutually exclusive mono-ubiquitination and mono-NEDDylation
inferred← citeshttps://doi.org/10.1111/gtc.12250openalex-snapshot
Protein monoubiquitylation: targets and diverse functions
inferred← citeshttps://doi.org/10.1128/jvi.00600-17openalex-snapshot
The Translesion Polymerase Pol η Is Required for Efficient Epstein-Barr Virus Infectivity and Is Regulated by the Viral Deubiquitinating Enzyme BPLF1
inferred← citeshttps://doi.org/10.1128/mcb.01152-14openalex-snapshot
The E3 Ubiquitin Ligase ARIH1 Protects against Genotoxic Stress by Initiating a 4EHP-Mediated mRNA Translation Arrest
inferred← citeshttps://doi.org/10.1242/dev.101196openalex-snapshot
TRIP/NOPO E3 ubiquitin ligase promotes ubiquitylation of DNA polymerase η
inferred← citeshttps://doi.org/10.1242/jcs.258637openalex-snapshot
DNA polymerase η is a substrate for calpain: A possible mechanism for pol η retention in UV induced replication foci
inferred← citeshttps://doi.org/10.1371/journal.pone.0080387openalex-snapshot
The Homeodomain Transcription Factor Hoxa2 Interacts with and Promotes the Proteasomal Degradation of the E3 Ubiquitin Protein Ligase RCHY1
inferred← citeshttps://doi.org/10.1371/journal.pone.0141347openalex-snapshot
Molecular Analysis of the HOXA2-Dependent Degradation of RCHY1
inferred← citeshttps://doi.org/10.1530/jme-15-0283openalex-snapshot
MuRF1 mono-ubiquitinates TRα to inhibit T3-induced cardiac hypertrophy in vivo
inferred← citeshttps://doi.org/10.21775/9781912530120.14openalex-snapshot
The Role of Ubiquitylation and SUMOylation in DNA Replication
inferred← citeshttps://doi.org/10.21775/cimb.040.189openalex-snapshot
The Role of Ubiquitination and SUMOylation in DNA Replication
inferred← citeshttps://doi.org/10.3123/jemsge.34.63openalex-snapshot
Human DNA Polymerase η and Its Regulatory Mechanisms
inferred← citeshttps://doi.org/10.3123/jemsge.34.89openalex-snapshot
Translesion DNA Synthesis and Hsp90
inferred← citeshttps://doi.org/10.3389/fgene.2016.00087openalex-snapshot
Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress
inferred← citeshttps://doi.org/10.3389/fgene.2016.00105openalex-snapshot
The Regulation of DNA Damage Tolerance by Ubiquitin and Ubiquitin-Like Modifiers
inferred← citeshttps://doi.org/10.3389/fonc.2021.822500openalex-snapshot
DNA Damage Tolerance Pathways in Human Cells: A Potential Therapeutic Target
inferred← citeshttps://doi.org/10.3390/cancers12102848openalex-snapshot
Ubiquitin and Ubiquitin-Like Proteins Are Essential Regulators of DNA Damage Bypass
inferred← citeshttps://doi.org/10.3390/cells11091515openalex-snapshot
The Role of E3 Ligase Pirh2 in Disease
inferred← citeshttps://doi.org/10.3390/genes15101271openalex-snapshot
Canonical and Non-Canonical Roles of Human DNA Polymerase η
inferred← citeshttps://doi.org/10.3390/genes8010019openalex-snapshot
Maintenance of Genome Integrity: How Mammalian Cells Orchestrate Genome Duplication by Coordinating Replicative and Specialized DNA Polymerases
inferred← citeshttps://doi.org/10.3390/genes8010024openalex-snapshot
Translesion Synthesis: Insights into the Selection and Switching of DNA Polymerases
inferred← citeshttps://doi.org/10.4161/cc.25785openalex-snapshot
Pirh2
inferred← citeshttps://doi.org/10.70675/2122f712z2f95z45caz8f82za68872f01e3copenalex-snapshot
La voie de dégradation CRL4Cdt2 régule le recrutement des ADN polymérases translésionnelles eta et kappa en foyers nucléaires après endommagements aux UV-C en ciblant pour dégradation les protéines qui contiennent des PIP box spécialisées
inferred← citeshttps://doi.org/10.70675/39007b42zbb49z41b5zb5ffz4d00c60c4b16openalex-snapshot
Formation et régulation du complexe polymérase du virus de la rougeole
inferred← citeshttps://doi.org/10.70675/cf32bcd5z3031z4693z8b1bz62fe76673cccopenalex-snapshot
Caractérisation fonctionnelle de la tolérance aux endommagements de l’ADN des embryons précoces
inferred← citeshttps://doi.org/10.7939/r3610vx4fopenalex-snapshot
The Role of Pirh2 E3 Ligases in Ubiquitination and p73 Regulation
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