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PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence

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What this work says

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

inferredcites →https://doi.org/10.1002/ijc.11124openalex-snapshot

EBV‐encoded EBNA‐5 associates with P14ARF in extranucleolar inclusions and prolongs the survival of P14ARF‐expressing cells

inferredcites →https://doi.org/10.1016/0092-8674(91)90113-dopenalex-snapshot

The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR

inferredcites →https://doi.org/10.1016/j.cell.2012.10.021openalex-snapshot

Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair

inferredcites →https://doi.org/10.1016/s0014-5793(02)03310-0openalex-snapshot

P14ARF promotes accumulation of SUMO‐1 conjugated (H)Mdm2

inferredcites →https://doi.org/10.1016/s1097-2765(01)00349-5openalex-snapshot

Involvement of PIAS1 in the Sumoylation of Tumor Suppressor p53

inferredcites →https://doi.org/10.1038/35018127openalex-snapshot

PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

inferredcites →https://doi.org/10.1038/35036365openalex-snapshot

The function of PML in p53-dependent apoptosis

inferredcites →https://doi.org/10.1038/cdd.2011.173openalex-snapshot

MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs

inferredcites →https://doi.org/10.1038/emboj.2011.370openalex-snapshot

Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence

inferredcites →https://doi.org/10.1038/ncb1147openalex-snapshot

PML regulates p53 stability by sequestering Mdm2 to the nucleolus

inferredcites →https://doi.org/10.1038/ncb1717openalex-snapshot

Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway

inferredcites →https://doi.org/10.1038/ncb3054openalex-snapshot

Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress

inferredcites →https://doi.org/10.1038/nm.3441openalex-snapshot

Activation of a promyelocytic leukemia–tumor protein 53 axis underlies acute promyelocytic leukemia cure

inferredcites →https://doi.org/10.1038/nrc3711openalex-snapshot

Unravelling mechanisms of p53-mediated tumour suppression

inferredcites →https://doi.org/10.1038/sj.onc.1204362openalex-snapshot

Functional analysis and intracellular localization of p53 modified by SUMO-1

inferredcites →https://doi.org/10.1038/sj.onc.1206851openalex-snapshot

MDM2-ARF complex regulates p53 sumoylation

inferredcites →https://doi.org/10.1073/pnas.0502978102openalex-snapshot

Sumoylation induced by the Arf tumor suppressor: A p53-independent function

inferredcites →https://doi.org/10.1073/pnas.0604800103openalex-snapshot

The promyelocytic leukemia protein functions as a negative regulator of IFN-γ signaling

inferredcites →https://doi.org/10.1073/pnas.1300490110openalex-snapshot

MOZ increases p53 acetylation and premature senescence through its complex formation with PML

inferredcites →https://doi.org/10.1074/jbc.m212215200openalex-snapshot

Physical and Functional Interactions between PML and MDM2

inferredcites →https://doi.org/10.1074/jbc.m301264200openalex-snapshot

The Promyelocytic Leukemia Protein Protects p53 from Mdm2-mediated Inhibition and Degradation

inferredcites →https://doi.org/10.1074/jbc.m710186200openalex-snapshot

Modification of Drosophila p53 by SUMO Modulates Its Transactivation and Pro-apoptotic Functions

inferredcites →https://doi.org/10.1083/jcb.147.2.221openalex-snapshot

Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1

inferredcites →https://doi.org/10.1083/jcb.201305148openalex-snapshot

Oxidative stress–induced assembly of PML nuclear bodies controls sumoylation of partner proteins

inferredcites →https://doi.org/10.1084/jem.193.12.1361openalex-snapshot

Role of Promyelocytic Leukemia (Pml) Sumolation in Nuclear Body Formation, 11s Proteasome Recruitment, and as2O3-Induced Pml or Pml/Retinoic Acid Receptor α Degradation

inferredcites →https://doi.org/10.1093/emboj/21.10.2383openalex-snapshot

Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence

inferredcites →https://doi.org/10.1093/emboj/cdf341openalex-snapshot

Deconstructing PML‐induced premature senescence

inferredcites →https://doi.org/10.1093/nar/gkg741openalex-snapshot

Identification of Daxx interacting with p73, one of the p53 family, and its regulation of p53 activity by competitive interaction with PML

inferredcites →https://doi.org/10.1101/cshperspect.a000661openalex-snapshot

PML Nuclear Bodies

inferredcites →https://doi.org/10.1101/gad.14.16.2015openalex-snapshot

PML is induced by oncogenic ras and promotes premature senescence

inferredcites →https://doi.org/10.1101/gad.827300openalex-snapshot

p53-independent functions of the p19ARF tumor suppressor

inferredcites →https://doi.org/10.1128/mcb.01064-14openalex-snapshot

TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification

inferredcites →https://doi.org/10.1158/0008-5472.can-05-3792openalex-snapshot

Characterization of Endogenous Human Promyelocytic Leukemia Isoforms

inferredcites →https://doi.org/10.1186/1476-4598-2-18openalex-snapshot

p14ARF induces the relocation of HDM2 and p53 to extranucleolar sites that are targeted by PML bodies and proteasomes.

inferredcites →https://doi.org/10.1242/jcs.007492openalex-snapshot

A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells

inferredcites →https://doi.org/10.1242/jcs.075390openalex-snapshot

PML isoforms I and II participate in PML-dependent restriction of HSV-1 replication

inferredcites →https://doi.org/10.1371/journal.ppat.1004512openalex-snapshot

Crystal Structure of Cytomegalovirus IE1 Protein Reveals Targeting of TRIM Family Member PML via Coiled-Coil Interactions

inferredcites →https://doi.org/10.1371/journal.ppat.1004785openalex-snapshot

Positive Role of Promyelocytic Leukemia Protein in Type I Interferon Response and Its Regulation by Human Cytomegalovirus

inferredcites →https://doi.org/10.3389/fonc.2013.00171openalex-snapshot

PML, SUMOylation, and Senescence

inferredcites →https://doi.org/10.4161/cc.25868openalex-snapshot

SUMOylation of p53 mediates interferon activities

inferredcites →https://doi.org/10.4161/cc.4.4.1588openalex-snapshot

p14ARF Interacts with the SUMO-Conjugating Enzyme Ubc9 and Promotes the Sumoylation of Its Binding Partners

inferredcites →https://doi.org/10.4161/cc.4.4.1597openalex-snapshot

MdmX Inhibits ARF Mediated Mdm2 Sumoylation

inferredcites →https://doi.org/10.4161/cc.6.6.4021openalex-snapshot

SUMO is Growing Senescent

inferredcites →https://doi.org/10.4161/cc.8.21.9954openalex-snapshot

Downregulation of ΔNp63α in keratinocytes by p14ARF-mediated SUMO-conjugation and degradation

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.3275284openalex-extracted

inferred← citeshttps://doi.org/10.1002/1873-3468.13717openalex-snapshot

Cell transformation by the adenovirus oncogenes E1 and E4

inferred← citeshttps://doi.org/10.1002/inmd.70120openalex-snapshot

SUMOylation regulates tumorigenesis and progression: Molecular mechanisms and therapeutic applications

inferred← citeshttps://doi.org/10.1002/jcb.29838openalex-snapshot

The SUMO‐specific protease SENP1 deSUMOylates p53 and regulates its activity

inferred← citeshttps://doi.org/10.1002/jcp.26862openalex-snapshot

PMLIV overexpression promotes TGF‐β‐associated epithelial–mesenchymal transition and migration in MCF‐7 cancer cells

inferred← citeshttps://doi.org/10.1007/978-3-319-50044-7_9openalex-snapshot

The Roles of SUMO in Metabolic Regulation

inferred← citeshttps://doi.org/10.1007/978-3-319-53168-7_4openalex-snapshot

The Human CMV IE1 Protein: An Offender of PML Nuclear Bodies

inferred← citeshttps://doi.org/10.1007/978-3-319-64257-4_2openalex-snapshot

Molecular Targets of Treatment in APL

inferred← citeshttps://doi.org/10.1007/978-3-319-64257-4_4openalex-snapshot

Molecular Genetics of APL

inferred← citeshttps://doi.org/10.1007/s00018-024-05452-4openalex-snapshot

SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved in the regulation of zinc metabolism in Golgi apparatus

inferred← citeshttps://doi.org/10.1016/j.bbrep.2024.101793openalex-snapshot

Unconventional localization of PAI-1 in PML bodies: A possible link with cellular growth of endothelial cells

inferred← citeshttps://doi.org/10.1016/j.ccell.2017.04.006openalex-snapshot

TRIB3 Promotes APL Progression through Stabilization of the Oncoprotein PML-RARα and Inhibition of p53-Mediated Senescence

inferred← citeshttps://doi.org/10.1016/j.ceb.2018.03.011openalex-snapshot

PML nuclear bodies: from architecture to function

inferred← citeshttps://doi.org/10.1016/j.cellin.2024.100199openalex-snapshot

The role of SUMOylation in biomolecular condensate dynamics and protein localization

inferred← citeshttps://doi.org/10.1016/j.cellsig.2024.111156openalex-snapshot

Unravelling the molecular interplay: SUMOylation, PML nuclear bodies and vascular cell activity in health and disease

inferred← citeshttps://doi.org/10.1016/j.cellsig.2026.112900openalex-snapshot

SUMOylation in skin homeostasis and disease: Regulation of cutaneous signaling networks

inferred← citeshttps://doi.org/10.1016/j.celrep.2020.108151openalex-snapshot

Endogenous Cyclin D1 Promotes the Rate of Onset and Magnitude of Mitogenic Signaling via Akt1 Ser473 Phosphorylation

inferred← citeshttps://doi.org/10.1016/j.dnarep.2022.103319openalex-snapshot

Phospho-SIM and exon8b of PML protein regulate formation of doxorubicin-induced rDNA-PML compartment

inferred← citeshttps://doi.org/10.1016/j.gendis.2020.07.003openalex-snapshot

Tumor suppressor p53 cross-talks with TRIM family proteins

inferred← citeshttps://doi.org/10.1016/j.isci.2026.115673openalex-snapshot

A ZNF-nanobody fusion reveals SUMOylation-dependent changes in p53 protein localization

inferred← citeshttps://doi.org/10.1016/j.jare.2025.06.028openalex-snapshot

SAE1 emerges as a pan-cancer driver and key regulator of HCC metastasis

inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110807openalex-snapshot

A short SUMOylation tag modulates transcription factor activity

inferred← citeshttps://doi.org/10.1016/j.mad.2017.01.002openalex-snapshot

The role of SUMOylation in ageing and senescent decline

inferred← citeshttps://doi.org/10.1016/j.pupt.2019.01.007openalex-snapshot

SUMOylation of Vps34 by SUMO1 promotes phenotypic switching of vascular smooth muscle cells by activating autophagy in pulmonary arterial hypertension

inferred← citeshttps://doi.org/10.1016/j.redox.2024.103073openalex-snapshot

Hypoxia causes trophoblast cell ferroptosis to induce miscarriage through lnc-HZ06/HIF1α-SUMO/NCOA4 axis

inferred← citeshttps://doi.org/10.1016/j.semcdb.2017.11.007openalex-snapshot

PML nuclear bodies, membrane-less domains acting as ROS sensors?

inferred← citeshttps://doi.org/10.1016/j.semcdb.2020.03.008openalex-snapshot

SUMOylation, a multifaceted regulatory mechanism in the pancreatic beta cells

inferred← citeshttps://doi.org/10.1016/j.semcdb.2021.10.012openalex-snapshot

Overview of the regulation of the class IA PI3K/AKT pathway by SUMO

inferred← citeshttps://doi.org/10.1016/j.tibs.2022.02.002openalex-snapshot

PML isoforms: a molecular basis for PML pleiotropic functions

inferred← citeshttps://doi.org/10.1038/cr.2016.86openalex-snapshot

The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death

inferred← citeshttps://doi.org/10.1038/s41388-018-0163-xopenalex-snapshot

Stability of HTLV-2 antisense protein is controlled by PML nuclear bodies in a SUMO-dependent manner

inferred← citeshttps://doi.org/10.1038/s41423-020-00564-wopenalex-snapshot

The SUMOylation of TAB2 mediated by TRIM60 inhibits MAPK/NF-κB activation and the innate immune response

inferred← citeshttps://doi.org/10.1038/s41467-022-33147-6openalex-snapshot

Exploration of nuclear body-enhanced sumoylation reveals that PML represses 2-cell features of embryonic stem cells

inferred← citeshttps://doi.org/10.1038/s41556-026-01894-zopenalex-snapshot

PML targets and resolves structured protein inclusions to mitigate neurodegeneration

inferred← citeshttps://doi.org/10.1038/s41598-018-25150-zopenalex-snapshot

Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9

inferred← citeshttps://doi.org/10.1038/s41598-020-57521-wopenalex-snapshot

Liquid-like droplet formation by tumor suppressor p53 induced by multivalent electrostatic interactions between two disordered domains

inferred← citeshttps://doi.org/10.1038/s41598-020-63779-xopenalex-snapshot

Interleukin-1α associates with the tumor suppressor p53 following DNA damage

inferred← citeshttps://doi.org/10.1038/s41598-020-72637-9openalex-snapshot

SUMO promotes longevity and maintains mitochondrial homeostasis during ageing in Caenorhabditis elegans

inferred← citeshttps://doi.org/10.1038/s42003-024-06232-3openalex-snapshot

SUMOylated Golgin45 associates with PML-NB to transcriptionally regulate lipid metabolism genes during heat shock stress

inferred← citeshttps://doi.org/10.1038/srep45038openalex-snapshot

PML nuclear bodies contribute to the basal expression of the mTOR inhibitor DDIT4

inferred← citeshttps://doi.org/10.1080/19491034.2024.2321265openalex-snapshot

PML Nuclear bodies: the cancer connection and beyond

inferred← citeshttps://doi.org/10.1080/19491034.2026.2646815openalex-snapshot

Discovery of novel murine PML isoforms

inferred← citeshttps://doi.org/10.1084/jem.20160301openalex-snapshot

PML is a ROS sensor activating p53 upon oxidative stress

inferred← citeshttps://doi.org/10.1084/jem.20201268openalex-snapshot

JAK2V617F myeloproliferative neoplasm eradication by a novel interferon/arsenic therapy involves PML

inferred← citeshttps://doi.org/10.1084/jem.20221213openalex-snapshot

The PML hub: An emerging actor of leukemia therapies

inferred← citeshttps://doi.org/10.1089/ars.2016.6898openalex-snapshot

Promyelocytic Leukemia Protein, a Protein at the Crossroad of Oxidative Stress and Metabolism

inferred← citeshttps://doi.org/10.1089/rej.2020.2406openalex-snapshot

SUMO Wrestles with Mitophagy to Extend Lifespan

inferred← citeshttps://doi.org/10.1096/fj.201901653ropenalex-snapshot

SUMO1 SUMOylates and SENP3 deSUMOylates NLRP3 to orchestrate the inflammasome activation

inferred← citeshttps://doi.org/10.1096/fj.202300216ropenalex-snapshot

Phase separation is required for PML nuclear body biogenesis and function

inferred← citeshttps://doi.org/10.1097/bs9.0000000000000034openalex-snapshot

PML nuclear body biogenesis and oligomerization-driven leukemogenesis

inferred← citeshttps://doi.org/10.1098/rsob.210050openalex-snapshot

SUMOylation modification-mediated cell death

inferred← citeshttps://doi.org/10.1101/cshperspect.a026260openalex-snapshot

p53 as an Effector or Inhibitor of Therapy Response

inferred← citeshttps://doi.org/10.1111/bjh.20255openalex-snapshot

A novel PML germline variant as a candidate predisposing genetic aberration in familial acute myeloid leukaemia

inferred← citeshttps://doi.org/10.1111/febs.15319openalex-snapshot

Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts

inferred← citeshttps://doi.org/10.1111/jcmm.16583openalex-snapshot

Krϋppel‐like factor 15 suppresses renal glomerular mesangial cell proliferation via enhancing P53 SUMO1 conjugation

inferred← citeshttps://doi.org/10.1128/mbio.02179-16openalex-snapshot

Promyelocytic Leukemia Protein (PML) ControlsListeria monocytogenesInfection

inferred← citeshttps://doi.org/10.1186/s12885-023-11603-wopenalex-snapshot

High expression of CDKN2A is associated with poor prognosis in colorectal cancer and may guide PD-1-mediated immunotherapy

inferred← citeshttps://doi.org/10.1186/s40164-022-00322-wopenalex-snapshot

TRIM family contribute to tumorigenesis, cancer development, and drug resistance

inferred← citeshttps://doi.org/10.1242/jcs.202879openalex-snapshot

C-terminal motifs in promyelocytic leukemia protein isoforms critically regulate PML nuclear body formation

inferred← citeshttps://doi.org/10.12659/msm.898616openalex-snapshot

P53 and Murine Double Mimute 2 (MDM2) Expression Changes and Significance in Different Types of Endometrial Lesions

inferred← citeshttps://doi.org/10.18297/etd/2539openalex-snapshot

The discovery of a novel, Ras-mediated NORE1A/PMLIV tumor suppressor complex.

inferred← citeshttps://doi.org/10.21203/rs.3.rs-125056/v1openalex-snapshot

Expression of Promyelocytic Leukemia (PML) Protein in the Mouse Developing Spermatogonia

inferred← citeshttps://doi.org/10.2174/1381612826666200622124134openalex-snapshot

Sumoylation as an Emerging Target in Therapeutics against Cancer

inferred← citeshttps://doi.org/10.3389/fcell.2022.818744openalex-snapshot

It’s Getting Complicated—A Fresh Look at p53-MDM2-ARF Triangle in Tumorigenesis and Cancer Therapy

inferred← citeshttps://doi.org/10.3390/biology12121511openalex-snapshot

Expanding Roles of the E2F-RB-p53 Pathway in Tumor Suppression

inferred← citeshttps://doi.org/10.3390/biom13121805openalex-snapshot

On the Prevalence and Roles of Proteins Undergoing Liquid–Liquid Phase Separation in the Biogenesis of PML-Bodies

inferred← citeshttps://doi.org/10.3390/cancers12030624openalex-snapshot

Acute Promyelocytic Leukemia: A Constellation of Molecular Events around a Single PML-RARA Fusion Gene

inferred← citeshttps://doi.org/10.3390/cancers14194549openalex-snapshot

Regulating the p53 Tumor Suppressor Network at PML Biomolecular Condensates

inferred← citeshttps://doi.org/10.3390/cancers16071351openalex-snapshot

History of Developing Acute Promyelocytic Leukemia Treatment and Role of Promyelocytic Leukemia Bodies

inferred← citeshttps://doi.org/10.3390/cells11050814openalex-snapshot

Sumoylation in Physiology, Pathology and Therapy

inferred← citeshttps://doi.org/10.3390/cimb48080751openalex-snapshot

SUMOylation-Driven Subtype Heterogeneity and Prognostic Biomarkers in Renal Cell Carcinoma

inferred← citeshttps://doi.org/10.3390/ijms22126289openalex-snapshot

PML Differentially Regulates Growth and Invasion in Brain Cancer

inferred← citeshttps://doi.org/10.3390/ijms23073480openalex-snapshot

The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer

inferred← citeshttps://doi.org/10.3390/ijms242316702openalex-snapshot

PML Body Biogenesis: A Delicate Balance of Interactions

inferred← citeshttps://doi.org/10.35702/onc.10012openalex-snapshot

Post-translational Modifications (PTMs), from a Cancer Perspective: An Overview

inferred← citeshttps://doi.org/10.3892/ijo.2018.4280openalex-snapshot

The post-translational modification, SUMOylation, and cancer (Review)

inferred← citeshttps://doi.org/10.3892/ijo.2021.5253openalex-snapshot

Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review)

inferred← citeshttps://doi.org/10.4000/annuaire-cdf.12819openalex-snapshot

Oncologie cellulaire et moléculaire

inferred← citeshttps://doi.org/10.4049/jimmunol.1800327openalex-snapshot

Tumor Suppressor p14ARF Enhances IFN-γ–Activated Immune Response by Inhibiting PIAS1 via SUMOylation

inferred← citeshttps://doi.org/10.4196/kjpp.2020.24.3.203openalex-snapshot

Interaction of promyelocytic leukemia/p53 affects signal transducer and activator of transcription-3 activity in response to oncostatin M

inferred← citeshttps://doi.org/10.70675/4f73d687z3c9fz4602zaad6z2808d59f1acbopenalex-snapshot

Caractérisation de l'effet des champs radiofréquences environnementaux sur les thermorécepteurs et sur la réponse globale des cellules au stress

inferred← citeshttps://doi.org/10.70675/70385a66zf181z4e65z9833z84f2ea720612openalex-snapshot

Mécanisme d’action de l’interféron dans le traitement des néoplasies myéloprolifératives JAK2V617F

inferred← citeshttps://doi.org/10.70675/793b0b93z9794z42d4zb8dfz5f3d68268a9bopenalex-snapshot

Rôle de FAT10 dans la sénescence des hépatocytes et le développement de la NASH

inferred← citeshttps://doi.org/10.70675/a97a0132zae2fz4278zad92z5e4b56df97b2openalex-snapshot

Identification of new regulators for PML nuclear bodies

inferred← citeshttps://doi.org/10.70675/b8e14224z7fb4z48a1zbe13zbd80a1788e94openalex-snapshot

A study on the role of PML in acute myeloid leukemia response to chemotherapy

inferred← citeshttps://doi.org/10.7150/ijbs.76214openalex-snapshot

Crosstalk between PML and p53 in response to TGF-β1: A new mechanism of cardiac fibroblast activation

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