ArticleMolecules and cells2012
The nuclear localization of glycogen synthase kinase 3β is required its putative PY-nuclear localization sequences.
Article in Molecules and cells, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- CMGC Kinases in Viral Infection and Human Disease.Pathogens (Basel, Switzerland) · 2026Review
- APC coordinates GSK3 phosphorylation of SETD8 to suppress colorectal cancer.Cell reports · 2026Article
- GSK3β/NF-κB -dependent transcriptional regulation of homeostatic hepatocyteAmerican journal of physiology. Gastrointestinal and liver physiology · 2024Article
- Interactomes of Glycogen Synthase Kinase-3 Isoforms.Journal of proteome research · 2023Article
- The ketone body β-hydroxybutyrate mitigates the senescence response of glomerular podocytes to diabetic insults.Kidney international · 2021Article
- Running Against the Wnt: How Wnt/β-Catenin Suppresses Adipogenesis.Frontiers in cell and developmental biology · 2021Review
- The stress response protein REDD1 promotes diabetes-induced oxidative stress in the retina by Keap1-independent Nrf2 degradation.The Journal of biological chemistry · 2020Article
- Review
- miR-632 Promotes Laryngeal Carcinoma Cell Proliferation, Migration, and Invasion Through Negative Regulation of GSK3β.Oncology research · 2020Article
- A nuclear shift of GSK3β protein is an independent prognostic factor in prostate cancer.Oncotarget · 2019Article
- Glycogen synthase kinase 3β inhibition enhanced proliferation, migration and functional re-endothelialization of endothelial progenitor cells in hypercholesterolemia microenvironment.Experimental biology and medicine (Maywood, N.J.) · 2015Article
- Article
- Article
- Phosphorylation of Tip60 Tyrosine 327 by Abl Kinase Inhibits HAT Activity through Association with FE65.The open biochemistry journal · 2013Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycogen synthase kinase-3β(GSK-3β), which is a member of the serine/threonine kinase family, has been shown to be crucial for cellular survival, differentiation, and metabolism. Here, we present evidence that GSK-3β is associated with the karyopherin β2 (Kap β2) (102-kDa), which functions as a substrate for transportation into the nucleus. A potential PY-NLS motif ((109)IVRLRYFFY(117)) was observed, which is similar with the consensus PY NLS motif (R/K/H)X(2-5)PY in the GSK-3β catalytic domain. Using a pull down approach, we observed that GSK-3β physically interacts with Kap β2 both in vivo and in vitro. Secondly, GSK-3β and Kap β2 were shown to be co-localized by confocal microscopy. The localization of GSK-3β to the nuclear region was disrupted by putative Kap β2 binding site mutation. Furthermore, in transient transfection assays, the Kap β2 binding site mutant induced a substantial reduction in the in vivo serine/threonine phosphorylation of GSK-3β, where- as the GSK-3β wild type did not. Thus, our observations indicated that Kap β2 imports GSK-3β through its putative PY NLS motif from the cytoplasm to the nucleus and increases its kinase activity.
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