Regulation of p53 family members by the ubiquitin-like SUMO system

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p53 in health and disease

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SUMO

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p53 ubiquitination: Mdm2 and beyond

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Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies

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PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

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Acetylation Is Indispensable for p53 Activation

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RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

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The Nucleoporin RanBP2 Has SUMO1 E3 Ligase Activity

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Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2

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

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SUMO‐1 modification activates the transcriptional response of p53

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Modification in reverse: the SUMO proteases

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Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity

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PIASy, a nuclear matrix–associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodiesPreprint

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p53: traffic cop at the crossroads of DNA repair and recombination

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PML is induced by oncogenic <i>ras</i> and promotes premature senescence

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The SUMO Pathway Is Essential for Nuclear Integrity and Chromosome Segregation in Mice

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The Mechanisms of PML-Nuclear Body Formation

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Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1

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Something about SUMO inhibits transcription

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Involvement of PIAS1 in the Sumoylation of Tumor Suppressor p53

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Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

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p63 mediates survival in squamous cell carcinoma by suppression of p73-dependent apoptosis

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TAp73 knockout shows genomic instability with infertility and tumor suppressor functionsPreprint

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c-Jun and p53 Activity Is Modulated by SUMO-1 Modification

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Covalent Modification of p73α by SUMO-1

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Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation

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Regulation of p53 activity in nuclear bodies by a specific PML isoform

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SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress

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The p53 family in differentiation and tumorigenesis

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The ubiquitin–protein ligase Itch regulates p73 stability

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Monoubiquitylation promotes mitochondrial p53 translocation

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PIAS/SUMO: new partners in transcriptional regulation

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SUMO: a regulator of gene expression and genome integrity

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SUMO-specific proteases: a twist in the tail

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E4F1 Is an Atypical Ubiquitin Ligase that Modulates p53 Effector Functions Independently of Degradation

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C-Terminal Ubiquitination of p53 Contributes to Nuclear Export

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Deconstructing PML‐induced premature senescence

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C-terminal modifications regulate MDM2 dissociation and nuclear export of p53

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A SIM-ultaneous role for SUMO and ubiquitin

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A C-Terminal Inhibitory Domain Controls the Activity of p63 by an Intramolecular Mechanism

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How important are post-translational modifications in p53 for selectivity in target-gene transcription and tumour suppression?

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Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest

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Role of ubiquitin- and Ubl-binding proteins in cell signaling

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Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53

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Topors acts as a SUMO‐1 E3 ligase for p53 in vitro and in vivo

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The Fast-Growing Business of SUMO Chains

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Sumo-1 Function Is Dispensable in Normal Mouse Development

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PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription

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PIAS proteins and transcriptional regulation—more than just SUMO E3 ligases?Preprint

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MDM2-ARF complex regulates p53 sumoylation

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

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The impact of p53 and p73 on aneuploidy and cancer

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Identification of SUMO-Dependent Chromatin-Associated Transcriptional Repression Components by a Genome-wide RNAi Screen

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The Protein Stability and Transcriptional Activity of p63α are Regulated by SUMO-1 Conjugation

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Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)

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PIAS-1 Is a Checkpoint Regulator Which Affects Exit from G1 and G2 by Sumoylation of p73

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A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis

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p53-Ubl fusions as models of ubiquitination, sumoylation and neddylation of p53

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The adenovirus E1B-55K oncoprotein induces SUMO modification of p53

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Destabilization of ΔNp63α by Nedd4-Mediated Ubiquitination Ubc9-Mediated Sumoylation, and Its Implications on Dorsoventral Patterning of the Zebrafish Embryo

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Altered Sumoylation of p63α Contributes to the Split-Hand/Foot Malformation Phenotype

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The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation

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Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

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

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Reconstitution of Mdm2-dependent post-translational modifications of p53 in yeast

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Degradation of p63 by Itch

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Multiple lysine mutations in the C-terminus of p53 make it resistant to degradation mediated by MDM2 but not by human papillomavirus E6 and induce growth inhibition in MDM2-overexpressing cells

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The nucleolus under stress

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The p53 orchestra: Mdm2 and Mdmx set the tone

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Regulating tumor suppressor genes: post-translational modifications

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p53 modifications: exquisite decorations of the powerful guardian

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Recent advances in our understanding of neurodegeneration

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p53 regulation by ubiquitin

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The role of ubiquitin modification in the regulation of p53

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Characterization of small ubiquitin-like modifier E3 ligase, OsSIZ1, mutant in rice

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SUMO playing tag with ubiquitin

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A SIM-ultaneous role for SUMO and ubiquitin

Perry, J. J. P., Tainer, J. A., & Boddy, M. N. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.02.001 · Cited by 224 · see citing works

CHFR is negatively regulated by SUMOylation-mediated ubiquitylation

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SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation

Rott, R., Szargel, R., Shani, V., Hamza, H., Savyon, M., Elghani, F. A., Bandopadhyay, R., & Engelender, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704351114 · Cited by 189 · see citing works