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DNA polymerase η is regulated by mutually exclusive mono-ubiquitination and mono-NEDDylation

https://doi.org/10.1101/2024.10.12.618026

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What this work says

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

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NMRPipe: A multidimensional spectral processing system based on UNIX pipes

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NEDDylation antagonizes ubiquitination of proliferating cell nuclear antigen and regulates the recruitment of polymerase η in response to oxidative DNA damage

inferredcites →https://doi.org/10.1016/j.bpj.2017.03.011openalex-snapshot

NMRbox: A Resource for Biomolecular NMR Computation

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Proteome-wide identification of NEDD8 modification sites reveals distinct proteomes for canonical and atypical NEDDylation

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DNA polymerase eta is targeted by Mdm2 for polyubiquitination and proteasomal degradation in response to ultraviolet irradiation

inferredcites →https://doi.org/10.1016/j.jmb.2015.09.014openalex-snapshot

The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes

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DNA Polymerase ι Interacts with Both the TRAF-like and UBL1-2 Domains of USP7

inferredcites →https://doi.org/10.1016/j.jmb.2023.168353openalex-snapshot

A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases

inferredcites →https://doi.org/10.1016/j.molcel.2007.05.014openalex-snapshot

E3-Independent Monoubiquitination of Ubiquitin-Binding Proteins

inferredcites →https://doi.org/10.1016/j.molcel.2008.04.011openalex-snapshot

DNA Polymerases at the Replication Fork in Eukaryotes

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.2013.01.006openalex-snapshot

RNF111-Dependent Neddylation Activates DNA Damage-Induced Ubiquitination

inferredcites →https://doi.org/10.1016/s1097-2765(01)00278-7openalex-snapshot

The Y-Family of DNA Polymerases

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The Structure of the APPBP1-UBA3-NEDD8-ATP Complex Reveals the Basis for Selective Ubiquitin-like Protein Activation by an E1

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University of California, San Francisco

inferredcites →https://doi.org/10.1021/bi500823hopenalex-snapshot

NMR Structure of the Human Rad18 Zinc Finger in Complex with Ubiquitin Defines a Class of UBZ Domains in Proteins Linked to the DNA Damage Response

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HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information

inferredcites →https://doi.org/10.1038/cr.2008.4openalex-snapshot

The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases

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An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer

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Regulation of ubiquitin-binding proteins by monoubiquitination

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Targeted inhibition of the COP9 signalosome for treatment of cancer

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Suffering in silence: the tolerance of DNA damage

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Y-family DNA polymerases and their role in tolerance of cellular DNA damage

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Accurate structure prediction of biomolecular interactions with AlphaFold 3

inferredcites →https://doi.org/10.1038/s41594-019-0370-3openalex-snapshot

Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics

inferredcites →https://doi.org/10.1038/s41598-019-41249-3openalex-snapshot

DNA polymerase ι is acetylated in response to SN2 alkylating agents

inferredcites →https://doi.org/10.1038/sj.emboj.7600383openalex-snapshot

Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

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/10.1038/sj.embor.7400901openalex-snapshot

Structure of the ubiquitin‐binding zinc finger domain of human DNA Y‐polymerase η

inferredcites →https://doi.org/10.1038/srep15759openalex-snapshot

Molecular architecture of the Ub-PCNA/Pol η complex bound to DNA

inferredcites →https://doi.org/10.1042/bj20111671openalex-snapshot

Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes

inferredcites →https://doi.org/10.1074/jbc.272.45.28557openalex-snapshot

Characterization of NEDD8, a Developmentally Down-regulated Ubiquitin-like Protein

inferredcites →https://doi.org/10.1074/jbc.273.52.34983openalex-snapshot

Crystal Structure of the Human Ubiquitin-like Protein NEDD8 and Interactions with Ubiquitin Pathway Enzymes

inferredcites →https://doi.org/10.1074/jbc.m303177200openalex-snapshot

Conservation in the Mechanism of Nedd8 Activation by the Human AppBp1-Uba3 Heterodimer

inferredcites →https://doi.org/10.1074/jbc.m809745200openalex-snapshot

Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear Antigen

inferredcites →https://doi.org/10.1093/emboj/18.12.3491openalex-snapshot

Xeroderma pigmentosum variant (XP‐V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity

inferredcites →https://doi.org/10.1093/nar/gkq239openalex-snapshot

Constitutive fusion of ubiquitin to PCNA provides DNA damage tolerance independent of translesion polymerase activities

inferredcites →https://doi.org/10.1093/nar/gks1277openalex-snapshot

Ubiquitin mediates the physical and functional interaction between human DNA polymerases η and ι

inferredcites →https://doi.org/10.1093/nar/gku1153openalex-snapshot

Ubiquitin recognition by FAAP20 expands the complex interface beyond the canonical UBZ domain

inferredcites →https://doi.org/10.1093/narcan/zcad005openalex-snapshot

Roles of trans-lesion synthesis (TLS) DNA polymerases in tumorigenesis and cancer therapy

inferredcites →https://doi.org/10.1111/febs.13734openalex-snapshot

A novel mode of ubiquitin recognition by the ubiquitin‐binding zinc finger domain of WRNIP 1

inferredcites →https://doi.org/10.1126/science.1120615openalex-snapshot

Ubiquitin-Binding Domains in Y-Family Polymerases Regulate Translesion Synthesis

inferredcites →https://doi.org/10.1128/mcb.01118-06openalex-snapshot

Ubiquitin-Binding Motifs in REV1 Protein Are Required for Its Role in the Tolerance of DNA Damage

inferredcites →https://doi.org/10.1128/mcb.05808-11openalex-snapshot

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

inferredcites →https://doi.org/10.1128/mmbr.00034-08openalex-snapshot

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

inferredcites →https://doi.org/10.1242/jcs.63.1.77openalex-snapshot

Limited and unlimited growth of sv40-transformed cells from human diploid mrc-5 fibroblasts

inferredcites →https://doi.org/10.1371/journal.pone.0120887openalex-snapshot

Structural Basis for Ubiquitin Recognition by Ubiquitin-Binding Zinc Finger of FAAP20

inferredcites →https://doi.org/10.3390/biom10040566openalex-snapshot

Old and New Concepts in Ubiquitin and NEDD8 Recognition

inferredcites →https://doi.org/10.3390/biom5042388openalex-snapshot

The Role of the COP9 Signalosome and Neddylation in DNA Damage Signaling and Repair

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Ubiquitin and Ubiquitin-Like Proteins Are Essential Regulators of DNA Damage Bypass

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