ArticlePloS one2012
Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- The impact of dysregulation SUMOylation on prostate cancer.Journal of translational medicine · 2025Review
- Post translational modification regulation of transcription factors governing pancreatic β-cell identity and functional mass.Frontiers in endocrinology · 2025Review
- Post-Translational Modifications That Drive Prostate Cancer Progression.Biomolecules · 2021Review
- Not So Slim Anymore-Evidence for the Role of SUMO in the Regulation of Lipid Metabolism.Biomolecules · 2020Review
- Inactivation of FOXA2 by Respiratory Bacterial Pathogens and Dysregulation of Pulmonary Mucus Homeostasis.Frontiers in immunology · 2020Review
- Functional characterization of recurrent FOXA2 mutations seen in endometrial cancers.International journal of cancer · 2018Article
- SUMOylation and phosphorylation cross-talk in hepatocellular carcinoma.Translational gastroenterology and hepatology · 2018Review
- The language-related transcription factor FOXP2 is post-translationally modified with small ubiquitin-like modifiers.Scientific reports · 2016Article
- The Key Regulator for Language and Speech Development, FOXP2, is a Novel Substrate for SUMOylation.Journal of cellular biochemistry · 2016Article
- Exploring the emerging complexity in transcriptional regulation of energy homeostasis.Nature reviews. Genetics · 2015Review
- Nuclear mobility and activity of FOXA1 with androgen receptor are regulated by SUMOylation.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Article
- The BTB-containing protein Kctd15 is SUMOylated in vivo.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The forkhead box protein A2 (FOXA2) is an important regulator of glucose and lipid metabolism and organismal energy balance. Little is known about how FOXA2 protein expression and activity are regulated by post-translational modifications. We have identified that FOXA2 is post-translationally modified by covalent attachment of a small ubiquitin related modifier-1 (SUMO-1) and mapped the sumoylation site to the amino acid lysine 6 (K6). Preventing sumoylation by mutating the SUMO acceptor K6 to arginine resulted in downregulation of FOXA2 protein but not RNA expression in INS-1E insulinoma cells. K6R mutation also downregulated FOXA2 protein levels in HepG2 hepatocellular carcinoma cells, HCT116 colon cancer cells and LNCaP and DU145 prostate cancer cells. Further, interfering with FOXA2 sumoylation through siRNA mediated knockdown of UBC9, an essential SUMO E2 conjugase, resulted in downregulation of FOXA2 protein levels. Stability of sumoylation deficient FOXA2K6R mutant protein was restored when SUMO-1 was fused in-frame. FOXA2 sumoylation and FOXA2 protein levels were increased by PIAS1 SUMO ligase but not a SUMO ligase activity deficient PIAS1 mutant. Although expressed at lower levels, sumoylation deficient FOXA2K6R mutant protein was detectable in the nucleus indicating that FOXA2 nuclear localization is independent of sumoylation. Sumoylation increased the transcriptional activity of FOXA2 on Pdx-1 area I enhancer. Together, our results show that sumoylation regulates FOXA2 protein expression and 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.