Cited by 163Alzheimer's disease research and treatmentsProtein Kinase Regulation and GTPase SignalingDementia and Cognitive Impairment Research

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Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro

Reynolds, C. Hugh, Nebreda, Angel R., Gibb, Graham M., Utton, Michelle A., Anderton, Brian H.·1997·Journal of Neurochemistry

DOI 10.1046/j.1471-4159.1997.69010191.x

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Abstract

Neurofibrillary tangles, one of the major pathological hallmarks of Alzheimer-diseased brains, consist primarily of aggregated paired helical filaments (PHFs) of hyperphosphorylated tau protein. Tau from normal brain and especially from foetal brain is also phosphorylated on some of the sites phosphorylated in PHFs, mainly at serines or threonines followed by prolines. A number of protein kinases can phosphorylate tau in vitro; those that require or accept prolines include GSK3 and members of the mitogen-activated protein (MAP) kinase family, ERK1, ERK2, and SAP kinase-beta/JNK. In this report, we show that another member of the MAP kinase family, the stress-activated kinase p38/RK, can phosphorylate tau in vitro. Western blots with phosphorylation-sensitive antibodies showed that p38, like ERK2 and SAP kinase-beta/JNK, phosphorylated tau at sites found phosphorylated physiologically (Thr181, Ser202, Thr205, and Ser396) and also at Ser422, which is phosphorylated in neurofibrillary tangles but not in normal adult or foetal brain. These findings support the possibility that cellular stress might contribute to tau hyperphosphorylation during the formation of PHFs, and hence, to the development of tau pathology.

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Authors: Reynolds, C. H., Nebreda, A. R., Gibb, G. M., Utton, M. A., & Anderton, B. H.
Affiliations: Guy's Hospital (GB)
Corresponding author: Reynolds, C. Hugh
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 1997-07
Volume: 69
Issue: 1
Pages: 191-198
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1046/j.1471-4159.1997.69010191.x
OpenAlex: W2013149569
Cited by: 161
References: 0
Citations by year: 2026: 1 · 2025: 1 · 2024: 5 · 2023: 13 · 2022: 7 · 2021: 2 · 2020: 2 · 2019: 1 · 2016: 3 · 2015: 3 · 2014: 6 · 2013: 6 · 2012: 5
FWCI: 3.82
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1966 d)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau phosphorylation, p38 MAPK, neurofibrillary tangles, paired helical filaments, Alzheimer's disease, ERK2, glycogen synthase kinase-3, stress-activated kinases, cellular stress, tau hyperphosphorylation
MeSH terms: Alzheimer Disease, Amino Acids, Antibody Specificity, Brain Chemistry, Humans, Neurons, Phosphorylation, Stress, Physiological, tau Proteins, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases

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Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro

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