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Cited by 287Alzheimer's disease research and treatmentsProtein Kinase Regulation and GTPase SignalingDementia and Cognitive Impairment Research

Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments.

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Paudel, H.K., Lew, J, Ali, Z, Wang, J.H.·1993·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)49492-1
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Abstract

Brain proline-directed protein kinase (BPDK), which contains a catalytic subunit homologous to and displaying site-specific phosphorylation similar to p34cdc2 kinase (Lew, J., Winkfein, R. J., Paudel, H. K., and Wang, J. H. (1992) J. Biol. Chem. 267, 25922-25926), has been examined for possible involvement in tau phosphorylation. Immunoblot analyses using peptide antibodies specific for BPDK have revealed the presence of the kinase in bovine brain microtubules purified extensively by repeated polymerization and depolymerization cycles. When the microtubule proteins are separated into the tubulin and microtubule-associated protein fractions, BPDK is found exclusively in the latter fraction. BPDK phosphorylates both tau and MAP2, the former protein being phosphorylated to a stoichiometry of 3.8 mol of phosphate/mol of tau. Analysis of the phosphopeptides isolated from the tryptic digest of the phosphorylated bovine tau has revealed seven phosphorylation sites. Based on the sequence alignment between bovine and human tau proteins, these sites correspond to Ser-195, Ser-202, Thr-205, Thr-231, Ser-235, Ser-396, and Ser-404 of human tau. Mass spectrometric analysis of the tau protein isolated from Alzheimer's paired helical filaments (PHFs) has determined three abnormal phosphorylation sites and two phosphopeptides containing a total of five abnormal phosphates (Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) J. Biol. Chem. 267, 17047-…

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  • 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 [14]

  • The results extend in vitro findings to an in vivo model system and indicate that GSK3β may be involved in tau phosphorylation in vivo.

    “They extend results obtained in vitro [7,12,14] to an in vivo model system, and indicate that GSK3fl may be involved in the phosphorylation of tau in vivo.”

    From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]

  • 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 [14]

  • GSK3β probably was directly responsible for the increased immunoreactivities and mobility shifts observed, because in vitro studies demonstrated that tau can be directly phosphorylated by GSK3β at many of the same sites.

    “However, since in vitro studies [7,12,14] have demonstrated that tau can be directly phosphorylated by GSK3fl at many of the sites we observed in transfected cells, GSK3fl probably was directly responsible for the increased immunoreactivities and mobility shifts observed here.”

    From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]

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Authors
Paudel, H. K., Lew, J., Ali, Z., & Wang, J. H.
Affiliations
University of Calgary (CA)
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-11
Volume
268
Issue
31
Pages
23512-23518
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)49492-1
OpenAlex
W1568595238
Cited by
285
References
49
Citations by year
2023: 4 · 2022: 3 · 2021: 2 · 2020: 1 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 2 · 2014: 5 · 2013: 7 · 2012: 6
FWCI
12.99
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Rare & Special e-Zone (The Hong Kong University of Science and Technology) (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 phosphorylation, paired helical filaments, Alzheimer's disease, MAP2, microtubule-associated proteins, phosphorylation sites
MeSH terms
Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cattle, Humans, Microtubule-Associated Proteins, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Phosphoserine, Phosphothreonine, tau Proteins, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Proline-Directed Protein Kinases

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