ArticleThe Journal of biological chemistry2011
Bioinformatic prediction and confirmation of beta-adducin as a novel substrate of glycogen synthase kinase 3.
Article in The Journal of biological chemistry, 2011. 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, 24 citations in OpenAlex.
- Upregulating ANKHD1 in PS19 Mice Reduces Tau Phosphorylation and Mitigates Tau Toxicity-Induced Cognitive Deficits.International journal of molecular sciences · 2025Article
- Glycogen Synthase Kinase 3: Ion Channels, Plasticity, and Diseases.International journal of molecular sciences · 2022Review
- IL-37-induced activation of glycogen synthase kinase 3β promotes IL-1R8/Sigirr phosphorylation, internalization, and degradation in lung epithelial cells.Journal of cellular physiology · 2021Article
- Integrated Proteogenomic Characterization across Major Histological Types of Pediatric Brain Cancer.Cell · 2020Article
- Phosphorylation of adducin-1 by cyclin-dependent kinase 5 is important for epidermal growth factor-induced cell migration.Scientific reports · 2019Article
- Reticulocyte and red blood cell deformation triggers specific phosphorylation events.Blood advances · 2019Article
- CK2 activity is required for the interaction of FGF14 with voltage-gated sodium channels and neuronal excitability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- The Nav1.2 channel is regulated by GSK3.Biochimica et biophysica acta · 2015Article
- Neuronal deletion of GSK3β increases microtubule speed in the growth cone and enhances axon regeneration via CRMP-2 and independently of MAP1B and CLASP2.BMC biology · 2014Article
- Glycogen synthase kinase 3 beta (GSK3β) at the tip of neuronal development and regeneration.Molecular neurobiology · 2014Review
- Serine phosphorylation of the insulin-like growth factor I (IGF-1) receptor C-terminal tail restrains kinase activity and cell growth.The Journal of biological chemistry · 2012Article
- GSK3 as a Sensor Determining Cell Fate in the Brain.Frontiers in molecular neuroscience · 2012Article
- Malignant glioma subset from actuate 1801: Phase I/II study of 9-ING-41, GSK-3β inhibitor, monotherapy or combined with chemotherapy for refractory malignancies.Neuro-oncology advancesArticle
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is important to identify the true substrates of protein kinases because this illuminates the primary function of any kinase. Here, we used bioinformatics and biochemical validation to identify novel brain substrates of the Ser/Thr kinase glycogen synthase kinase 3 (GSK3). Briefly, sequence databases were searched for proteins containing a conserved GSK3 phosphorylation consensus sequence ((S/T)PXX(S/T)P or (S/T)PXXX(S/T)P), as well as other criteria of interest (e.g. brain proteins). Importantly, candidates were highlighted if they had previously been reported to be phosphorylated at these sites by large-scale phosphoproteomic studies. These criteria identified the brain-enriched cytoskeleton-associated protein β-adducin as a likely substrate of GSK3. To confirm this experimentally, it was cloned and subjected to a combination of cell culture and in vitro kinase assays that demonstrated direct phosphorylation by GSK3 in vitro and in cells. Phosphosites were mapped to three separate regions near the C terminus and confirmed using phosphospecific antibodies. Prior priming phosphorylation by Cdk5 enhanced phosphorylation by GSK3. Expression of wild type, but not non-phosphorylatable (GSK3 insensitive), β-adducin increased axon and dendrite elongation in primary cortical neurons. Therefore, phosphorylation of β-adducin by GSK3 promotes efficient neurite outgrowth in neurons.
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Registered trials
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