ArticlePloS one2011
SUMOylation of the Forkhead transcription factor FOXL2 promotes its stabilization/activation through transient recruitment to PML bodies.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Modification of the Transcription Factor FOXL2 at Serines 101 and 107 Disables DNA Binding, Leads to Nucleolar Relocalization, and Rewires Granulosa-Cell Programs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Conditional ablation of Insr and Igf1r using Esr2-Cre leads to abnormal ovarian follicle development and infertility in mice†.Biology of reproduction · 2025Article
- Sex-specific expression and function of TRIM28 during mouse primordial germ differentiation.iScience · 2025Article
- Comprehensive SUMO Proteomic Analyses Identify HIV Latency-Associated Proteins in Microglia.Cells · 2025Article
- Postnatal Ovarian Transdifferentiation in the Absence of Estrogen Receptor Signaling Is Dependent on Genetic Background.Endocrinology · 2024Article
- On the Prevalence and Roles of Proteins Undergoing Liquid-Liquid Phase Separation in the Biogenesis of PML-Bodies.Biomolecules · 2023Article
- TRIM28-dependent SUMOylation protects the adult ovary from activation of the testicular pathway.Nature communications · 2022Article
- Not So Slim Anymore-Evidence for the Role of SUMO in the Regulation of Lipid Metabolism.Biomolecules · 2020Review
- FOXL2 directs DNA double-strand break repair pathways by differentially interacting with Ku.Nature communications · 2020Article
- Article
- Prostaglandin E2 (PGE2) promotes proliferation and invasion by enhancing SUMO-1 activity via EP4 receptor in endometrial cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Novel action of FOXL2 as mediator of Col1a2 gene autoregulation.Developmental biology · 2016Article
- Combined comparative genomic hybridization and transcriptomic analyses of ovarian granulosa cell tumors point to novel candidate driver genes.BMC cancer · 2015Article
- FOXL2 transcriptionally represses Sf1 expression by antagonizing WT1 during ovarian development in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Article
- Essential but differential role of FOXL2wt and FOXL2C134W in GDF-9 stimulation of follistatin transcription in co-operation with Smad3 in the human granulosa cell line COV434.Molecular and cellular endocrinology · 2013Article
- PIASγ enhanced SUMO-2 modification of Nurr1 activation-function-1 domain limits Nurr1 transcriptional synergy.PloS one · 2013Article
- SUMOylation represses Nanog expression via modulating transcription factors Oct4 and Sox2.PloS one · 2012Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundFOXL2 is a transcription factor essential for ovarian development and maintenance. It is mutated in the genetic condition called Blepharophimosis Ptosis Epicantus inversus Syndrome (BPES) and in cases of isolated premature ovarian failure. We and others have previously shown that FOXL2 undergoes several post-translational modifications. METHODS AND PRINCIPAL
findingsHere, using cells in culture, we show that interference with FOXL2 SUMOylation leads to a robust inhibition of its transactivation ability, which correlates with a decreased stability. Interestingly, FOXL2 SUMOylation promotes its transient recruitment to subnuclear structures that we demonstrate to be PML (Promyelocytic Leukemia) Nuclear Bodies. Since PML bodies are known to be sites where post-translational modifications of nuclear factors take place, we used tandem mass spectrometry to identify new post-translational modifications of FOXL2. Specifically, we detected four phosphorylated, one sulfated and three acetylated sites.
conclusionsBy analogy with other transcription factors, we propose that PML Nuclear Bodies might transiently recruit FOXL2 to the vicinity of locally concentrated enzymes that could be involved in the post-translational maturation of FOXL2. FOXL2 acetylation, sulfation, phosphorylation as well as other modifications yet to be discovered might alter the transactivation capacity of FOXL2 and/or its stability, thus modulating its global intracellular activity.
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