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Cited by 565Alzheimer's disease research and treatmentsProtein Kinase Regulation and GTPase SignalingDementia and Cognitive Impairment Research

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

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Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E.M., Biernat, J., Goris, J., Dorée, M., Mandelkow, E.·1992·The EMBO Journal
DOI 10.1002/j.1460-2075.1992.tb05272.xPMC PMC556680
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Abstract

The microtubule-associated protein tau is a major component of the paired helical filaments (PHFs) observed in Alzheimer's disease brains. The pathological tau is distinguished from normal tau by its state of phosphorylation, higher apparent M(r) and reaction with certain antibodies. However, the protein kinase(s) have not been characterized so far. Here we describe a protein kinase from brain which specifically induces the Alzheimer-like state in tau protein. The 42 kDa protein belongs to the family of mitogen activated protein kinases (MAPKs) and is activated by tyrosine phosphorylation. It is capable of phosphorylating Ser-Pro and Thr-Pro motifs in tau protein (approximately 14-16 P1 per tau molecule). By contrast, other proline directed Ser/Thr kinases such as p34(cdc2) combined with cyclin A or B have only minor effects on tau phosphorylation. We propose that MAP kinase is abnormally active in Alzheimer brain tissue, or that the corresponding phosphatases are abnormally passive, due to a breakdown of the normal regulatory mechanisms.

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Crossref · 10.1002/j.1460-2075.1992.tb05272.x

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  • MAP kinase, GSK3, and neuronal cdc2-like kinase (cdk5) have been shown to phosphorylate tau in vitro at sites that are phosphorylated in PHFs.

    “Mitogen-activated protein kinase, glycogen synthase kinase-3 (GSK3) and neuronal cdc2-1ike kinase have been shown to phosphorylate tau protein in vitro at a number of sites that are phosphorylated in PHFs.”

    From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [2]

    The passage labeled Abstract in our indexed copy reports that MAP kinase phosphorylates tau and induces an Alzheimer-like state. It does not establish the claim for GSK3 or neuronal cdc2-like kinase (cdk5), and the passages retrieved for those terms provide no such result. The copy instead says that p34(cdc2) with cyclin A or B has only minor effects on tau phosphorylation; it does not identify p34(cdc2) as cdk5. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • ERK can phosphorylate tau, and elevated activity of MAPK/ERK has been reported in several tauopathies and may play a role in early stages of NFT formation.

    “ERK can phosphorylate tau (29), and elevated activity of MAPK/ERK has been reported in several tauopathies and may play a role in early stages of neurofibriliary tangle (NFT) formation (82,130,131).”

    From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [29]

  • Prior studies of tau phosphorylation by these kinases were carried out in vitro without exception.

    “However, without exception, these studies have been carried out in vitro.”

    From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [2]

    The indexed copy’s Full text section lists PDF page images rather than readable passages from the paper’s body. Searches for in vitro and in vivo tau phosphorylation found no passage stating that all prior studies of phosphorylation by these kinases were conducted in vitro; the reference list cannot establish the 'without exception' claim. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E.
Affiliations
Max Planck Unit for Structural Molecular Biology (DE)
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
1992-06-01
Volume
11
Issue
6
Pages
2131-2138
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
DOI
10.1002/j.1460-2075.1992.tb05272.x
PMC
PMC556680
OpenAlex
W2167241481
Cited by
565
References
1
Citations by year
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FWCI
36.79
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • DESY (CERN, DESY, Fermilab, IHEP, and SLAC) (submittedVersion)
Topics
  • Health Sciences › Medicine › Physiology › 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 protein, mitogen-activated protein kinase, Alzheimer's disease, tau phosphorylation, paired helical filaments, tyrosine phosphorylation, protein kinases, p34cdc2, cyclin A, cyclin B, protein phosphorylation
MeSH terms
Alzheimer Disease, Animals, Brain, Cattle, Chromatography, Ion Exchange, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Humans, Molecular Weight, Phosphorylation, Protein Kinases, Recombinant Proteins, Reference Values, Substrate Specificity, Swine, Tyrosine, tau Proteins, Calcium-Calmodulin-Dependent Protein Kinases, Phosphotyrosine

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