ArticleOncogene2006
The promyelocytic leukemia protein stimulates SUMO conjugation in yeast.
Article in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
- SUMOylation in Viral Replication and Antiviral Defense.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- The Fate of Speckled Protein 100 (Sp100) During Herpesviruses Infection.Frontiers in cellular and infection microbiology · 2020Review
- Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Pml nuclear body disruption cooperates in APL pathogenesis and impairs DNA damage repair pathways in mice.Blood · 2018Article
- A versatile plasmid system for reconstitution and analysis of mammalian ubiquitination cascades in yeast.Microbial cell (Graz, Austria) · 2017Article
- The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus.Journal of virology · 2017Article
- The Human Cytomegalovirus IE1 Protein Antagonizes PML Nuclear Body-Mediated Intrinsic Immunity via the Inhibition of PML De Novo SUMOylation.Journal of virology · 2017Article
- A Phospho-SIM in the Antiviral Protein PML is Required for Its Recruitment to HSV-1 Genomes.Cells · 2014Article
- Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins.The Journal of cell biology · 2014Article
- Article
- PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation.Nucleus (Austin, Tex.) · 2014Review
- The role of small ubiquitin-like modifier-interacting motif in the assembly and regulation of metal-responsive transcription factor 1.The Journal of biological chemistry · 2011Article
- Motor neuron impairment mediated by a sumoylated fragment of the glial glutamate transporter EAAT2.Glia · 2011Article
- SUMO E3 ligase activity of TRIM proteins.Oncogene · 2011Article
- Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies.Molecular biology of the cell · 2010Article
- PML nuclear bodies.Cold Spring Harbor perspectives in biology · 2010Review
- A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.International journal of biological sciences · 2010Review
- KRAB zinc-finger proteins localise to novel KAP1-containing foci that are adjacent to PML nuclear bodies.Journal of cell science · 2009Article
- Pondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon?Biochimica et biophysica acta · 2008Review
- Cooperation of sumoylated chromosomal proteins in rDNA maintenance.PLoS genetics · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The promyelocytic leukemia gene was first identified through its fusion to the gene encoding the retinoic acid receptor alpha (RARalpha) in acute promyelocytic leukemia (APL) patients. The promyelocytic leukemia gene product (PML) becomes conjugated in vivo to the small ubiquitin-like protein SUMO-1, altering its behavior and capacity to recruit other proteins to PML nuclear bodies (PML-NBs). In the NB4 cell line, which was derived from an APL patient and expresses PML:RARalpha, we observed a retinoic acid-dependent change in the modification of specific proteins by SUMO-1. To dissect the interaction of PML with the SUMO-1 modification pathway, we used the budding yeast Saccharomyces cerevisiae as a model system through expression of PML and human SUMO-1 (hSUMO-1). We found that PML stimulated hSUMO-1 modification in yeast, in a manner that was dependent upon PML's RING-finger domain. PML:RARalpha also stimulated hSUMO-1 conjugation in yeast. Interestingly, however, PML and PML:RARalpha differentially complemented yeast Smt3p conjugation pathway mutants. These findings point toward a potential function of PML and PML:RARalpha as SUMO E3 enzymes or E3 regulators, and suggest that fusion of RARalpha to PML may affect this activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.