ArticleMolecular biology of the cell2011
The SUMO protease SENP6 is a direct regulator of PML nuclear bodies.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 75 citations in OpenAlex.
- DNA double strand break repair: a model of specificity and complexity in SUMO signalling.Essays in biochemistry · 2025Review
- SENP6 Maintains Mitochondrial Homeostasis by Regulating Mitochondrial Protein Import Through deSUMOylation of TOM40.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- UBC9-Mediated SUMO Pathway Drives Prohibitin-1 Nuclear Accumulation and PITX1 Repression in Primary Osteoarthritis.International journal of molecular sciences · 2025Article
- SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The role of SUMOylation in biomolecular condensate dynamics and protein localization.Cell insight · 2024Review
- Stepwise phosphorylation and SUMOylation of PIDD1 drive PIDDosome assembly in response to DNA repair failure.Nature communications · 2024Article
- Mechanisms and functions of SUMOylation in health and disease: a review focusing on immune cells.Journal of biomedical science · 2024Review
- On the Prevalence and Roles of Proteins Undergoing Liquid-Liquid Phase Separation in the Biogenesis of PML-Bodies.Biomolecules · 2023Article
- SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation.Nature communications · 2023Article
- Histone demethylase KDM2A is a selective vulnerability of cancers relying on alternative telomere maintenance.Nature communications · 2023Article
- In-Plate Chemical Synthesis of Isopeptide-Linked SUMOylated Peptide Fluorescence Polarization Reagents for High-Throughput Screening of SENP Preferences.Chembiochem : a European journal of chemical biology · 2023Article
- Effects of arsenic on the topology and solubility of promyelocytic leukemia (PML)-nuclear bodies.PloS one · 2022Article
- Running 'LAPS' Around nLD: Nuclear Lipid Droplet Form and Function.Frontiers in cell and developmental biology · 2022Review
- Regulation of transforming growth factor-β signalling by SUMOylation and its role in fibrosis.Open biology · 2021Article
- SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease.Frontiers in molecular biosciences · 2021Review
- Photobody Detection Using Immunofluorescence and Super-Resolution Imaging in Arabidopsis.Methods in molecular biology (Clifton, N.J.) · 2021Article
- SUMO: Glue or Solvent for Phase-Separated Ribonucleoprotein Complexes and Molecular Condensates?Frontiers in molecular biosciences · 2021Review
- An Insight into the Factors Influencing Specificity of the SUMO System in Plants.Plants (Basel, Switzerland) · 2020Review
- PML hyposumoylation is responsible for the resistance of pancreatic cancer.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation.Nature communications · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Promyelocytic leukemia protein (PML) is the core component of PML-nuclear bodies (PML NBs). The small ubiquitin-like modifier (SUMO) system (and, in particular, SUMOylation of PML) is a critical component in the formation and regulation of PML NBs. SUMO protease SENP6 has been shown previously to be specific for SUMO-2/3-modified substrates and shows preference for SUMO polymers. Here, we further investigate the substrate specificity of SENP6 and show that it is also capable of cleaving mixed chains of SUMO-1 and SUMO-2/3. Depletion of SENP6 results in accumulation of endogenous SUMO-2/3 and SUMO-1 conjugates, and immunofluorescence analysis shows accumulation of SUMO and PML in an increased number of PML NBs. Although SENP6 depletion drastically increases the size of PML NBs, the organizational structure of the body is not affected. Mutation of the catalytic cysteine of SENP6 results in its accumulation in PML NBs, and biochemical analysis indicates that SUMO-modified PML is a substrate of SENP6.
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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.