GSK3: a possible link between beta amyloid peptide and tau protein
Abstract
Tau is a neuronal microtubule-associated phosphoprotein that is highly phosphorylated by glycogen synthase kinase 3 (GSK3). Tau phosphorylation by GSK3 regulates tau binding to microtubules, tau degradation and tau aggregation. Tau phosphorylation is important in Alzheimer disease pathology and in other tauopathies. In Alzheimer disease, it has been proposed that the peptide beta amyloid promotes GSK3 activation, resulting in tau phosphorylation. In this work, we review the links between beta amyloid peptide, tau protein and GSK3 that occur in familial Alzheimer disease. We also discuss the possible links between GSK3 and sporadic Alzheimer disease. Finally, we include a brief review of the pathology of animal models overexpressing GSK3.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
GSK3 is a proline-directed kinase that contributes to phosphorylation of tau at SP/TP sites.
“GSK3 is a proline-directed kinase that contributes to phosphorylation of tau at serine or threonine followed by proline (i.e., SP/TP sites) [46–49]”
Cites
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560 · see citing works
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 735 · see citing works
Neurons May Live for Decades with Neurofibrillary Tangles
Morsch, R., Simon, W., & Coleman, P. D. (1999) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199902000-00008 · Cited by 370 · see citing works
Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90063-w · Cited by 332 · see citing works
Soluble Aβ Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway
Townsend, M., Mehta, T., & Selkoe, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610390200 · Cited by 318 · see citing works
Johnson, G. V. W., Jope, R. S., & Binder, L. I. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91150-9 · Cited by 161 · see citing works
Association of GSK3B with Alzheimer disease and frontotemporal dementia
Schaffer, B. A. J., Bertram, L., Miller, B. L., Mullin, K., Weintraub, S., Johnson, N., Bigio, E. H., Mesulam, M., Wiedau-Pazos, M., Jackson, G. R., et al. (2008) · Archives of Neurology · doi:10.1001/archneur.65.10.1368 · Cited by 100 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Tau protein kinases: Involvement in Alzheimer's disease
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622 · see citing works
“While this phenomenon may result from the direct cross-seeding of tau by aggregated A β 71, 72 , indirect pathways such as A β -induced tau phosphorylation, inflammation, and/or disruption of proteostasis 20, 73-75 have not been ruled out.”
BackgroundNatural products as a source of Alzheimer's drug leads
Williams, P., Sorribas, A., & Howes, M.-J. R. (2011) · Nat. Prod. Rep. · doi:10.1039/c0np00027b · Cited by 404 · see citing works
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331 · see citing works
Neuroprotective effect of natural products against Alzheimer’s disease
Essa, M. M., Vijayan, R. K., Castellano-Gonzalez, G., Memon, M. A., Braidy, N., & Guillemin, G. J. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0799-9 · Cited by 278 · see citing works
Ma, T., Hoeffer, C. A., Capetillo-Zarate, E., Yu, F., Wong, H., Lin, M. T., Tampellini, D., Klann, E., Blitzer, R. D., & Gouras, G. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012845 · Cited by 262 · see citing works
Vallée, A., Lecarpentier, Y., Guillevin, R., & Vallée, J.-N. (2017) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx073 · Cited by 226 · see citing works
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220 · see citing works
Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105 · see citing works
Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells
Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S., & Morfini, G. (2012) · Experimental Brain Research · doi:10.1007/s00221-011-2870-1 · Cited by 92 · see citing works
Ciccone, L., Shi, C., di Lorenzo, D., Van Baelen, A.-C., & Tonali, N. (2020) · Molecules · doi:10.3390/molecules25102439 · Cited by 69 · see citing works
Role of GSK-3β Inhibitors: New Promises and Opportunities for Alzheimer’s Disease
Shri, S. R., Manandhar, S., Nayak, Y., & Pai, K. S. R. (2023) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.071 · Cited by 71 · see citing works
Zhang, H., Lin, A., Gong, P., Chen, Y., Ye, R. D., Qian, F., Zhang, Y., & Yu, Y. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0455-20.2020 · Cited by 24 · see citing works
Hasan, N., Zameer, S., Najmi, A. K., Parvez, S., & Akhtar, M. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00482-x · Cited by 17 · see citing works
Retracted
- Authors
- Hernández, F., Gómez de Barreda, E., Fuster-Matanzo, A., Lucas, J. J., & Avila, J.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Venue
- Experimental Neurology
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 223
- Issue
- 2
- Pages
- 322-325
- ISSN
- 0014-4886 (ISSN-L)
- OpenAlex
- W2112896415
- Cited by
- 327
- References
- 7
- Citations by year
- 2026: 11 · 2025: 23 · 2024: 30 · 2023: 14 · 2022: 20 · 2021: 22 · 2020: 26 · 2019: 13 · 2018: 11 · 2017: 19 · 2016: 16 · 2015: 5 · 2014: 25 · 2013: 28 · 2012: 28
- FWCI
- 2.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Experimental Neurology (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Funders
- Comunidad de Madrid
- Comisión Interministerial de Ciencia y Tecnología
- Fundación Ramón Areces
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- glycogen synthase kinase-3, beta-amyloid peptide, tau protein, tau phosphorylation, Alzheimer's disease, familial Alzheimer's disease, sporadic Alzheimer's disease, tauopathy, tau aggregation, microtubule binding
- MeSH terms
- Alzheimer Disease, Animals, Brain, Disease Models, Animal, Humans, Phosphorylation, Amyloid beta-Peptides, tau Proteins, Glycogen Synthase Kinase 3
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
