Cited by 201Alzheimer's disease research and treatmentsCalpain Protease Function and RegulationS100 Proteins and Annexins

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Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.

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Litersky, J M, Johnson, G V·1992·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)45982-0

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Abstract

The effects of cAMP-dependent protein kinase (cAMP-PK) phosphorylation on the degradation of the microtubule-associated protein tau by calpain were studied. Purified bovine brain tau that had been phosphorylated by cAMP-PK had a slower migration pattern on sodium dodecyl sulfate-polyacrylamide gels and a more acidic, less heterogeneous pattern on two-dimensional, nonequilibrium pH gradient electrophoresis (NEPHGE) gels compared with untreated tau. Phosphorylation of tau by cAMP-PK significantly inhibited its proteolysis by calpain compared with untreated tau. To our knowledge this is the first demonstration that phosphorylation of tau by a specific kinase results in increased resistance to hydrolysis by calpain. Tau dephosphorylated by alkaline phosphatase migrated more rapidly on sodium dodecyl sulfate-polyacrylamide gels and also showed an altered two-dimensional NEPHGE pattern. Dephosphorylation of tau had no effect on its susceptibility to calpain proteolysis, indicating that regulation of the susceptibility to calpain hydrolysis is due to the phosphorylation of a specific site(s). These results suggest a role for phosphorylation in regulating the degradation of tau. Abnormal phosphorylation could result in a protease-resistant tau population which may contribute to the formation of paired helical filaments in Alzheimer's disease.

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Authors: Litersky, J. M., & Johnson, G. V.
Affiliations: University of Alabama (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-01
Volume: 267
Issue: 3
Pages: 1563-1568
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)45982-0
OpenAlex: W1531327859
Cited by: 201
References: 52
Citations by year: 2026: 1 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 2 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 3 · 2013: 4 · 2012: 6
FWCI: 8.21
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10545 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ag006569-13)
National Institute on Aging (AG06569)
National Institute of Neurological Disorders and Stroke (NS-27538)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Keywords: tau protein, protein kinase A, phosphorylation, calpain, proteolysis, microtubule-associated proteins, dephosphorylation, protease resistance, Alzheimer's disease, paired helical filaments
MeSH terms: Animals, Autoradiography, Brain, Calpain, Cattle, Electrophoresis, Polyacrylamide Gel, Kinetics, Microtubules, Phosphorus Radioisotopes, Phosphorylation, Protein Kinases, Immunoblotting, Electrophoresis, Gel, Two-Dimensional, tau Proteins

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Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.

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