ArticleThe open biochemistry journal2008
Regulation of glycogen synthase kinase 3beta functions by modification of the small ubiquitin-like modifier.
Article in The open biochemistry journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- PIAS1-mediated GSK3β SUMOylation exacerbates tauopathy and cognitive deficits in Alzheimer's disease models.Molecular psychiatry · 2026Article
- SUMOylation balance: a key determinant in synapse physiology.Frontiers in physiology · 2025Review
- Review
- Regulation of SUMOylation Targets Associated With Wnt/β-Catenin Pathway.Frontiers in oncology · 2022Review
- Review
- Novel SUMO-Protease SENP7S Regulates β-catenin Signaling and Mammary Epithelial Cell Transformation.Scientific reports · 2017Article
- SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017Article
- Battling Alzheimer's Disease: Targeting SUMOylation-Mediated Pathways.Neurochemical research · 2016Review
- SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Physiological reviews · 2014Review
- Regulation of Wnt/β-catenin signaling by posttranslational modifications.Cell & bioscience · 2014Article
- SUMO and Alzheimer's disease.Neuromolecular medicine · 2013Review
- Receptor trafficking and the regulation of synaptic plasticity by SUMO.Neuromolecular medicine · 2013Review
- The nuclear localization of glycogen synthase kinase 3β is required its putative PY-nuclear localization sequences.Molecules and cells · 2012Article
- Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation.Biomolecules · 2012Article
- Targets and consequences of protein SUMOylation in neurons.Brain research reviews · 2010Review
- Mechanisms, regulation and consequences of protein SUMOylation.The Biochemical journal · 2010Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modification of the Small Ubiquitin-like Modifier (SUMO) (SUMOylation) appears to regulate diverse cellular processes, including nuclear transport, signal transduction, apoptosis, autophagy, cell cycle control, ubiquitin-dependent degradation and gene transcription. Glycogen synthase kinase 3beta (GSK 3beta) is a serine/threonine kinase that is thought to contribute to a variety of biological events, including embryonic development, metabolism, tumorigenesis, and cell death. GSK 3beta is a constitutively active kinase that regulates many intracellular signaling pathways by phosphorylating substrates such as beta-catenin. We noticed that the putative SUMOylation sites are localized on K(292 )residueof (291)FKFPQ(295) in GSK 3beta based on analysis of the SUMOylation consensus sequence. In this report, we showed that the SUMOylation of GSK 3beta occurs on its K(292) residue, and this modification promotes its nuclear localization in COS-1. Additionally, our data showed that the GSK 3beta SUMO mutant (K292R) decreased its kinase activity and protein stability, affecting cell death. Therefore, our observations at first time suggested that SUMOylation on the K(292) residue of GSK 3beta might be a GSK 3beta regulation mechanism for its kinase activation, subcellular localization, protein stability, and cell apoptosis.
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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.