Phosphorylation of tau by proline-directed protein kinase (p34cdc2/p58cyclin A) decreases tau-induced microtubule assembly and antibody SMI33 reactivity
| Autor: | Claudia B. Caputo, Clay W Scott, P.Richard Vulliet |
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| Rok vydání: | 1993 |
| Předmět: |
inorganic chemicals
Microtubule-associated protein Molecular Sequence Data Tau protein tau Proteins Antigen-Antibody Complex macromolecular substances Microtubules environment and public health Antibodies Phosphoamino acid analysis Substrate Specificity MAP2K7 Cyclins CDC2 Protein Kinase Humans Protein phosphorylation Amino Acid Sequence Phosphorylation Protein kinase A Molecular Biology biology General Neuroscience Recombinant Proteins enzymes and coenzymes (carbohydrates) Biochemistry biology.protein bacteria Neurology (clinical) Developmental Biology |
| Zdroj: | Brain Research. 611:237-242 |
| ISSN: | 0006-8993 |
| DOI: | 10.1016/0006-8993(93)90508-k |
| Popis: | Tau protein was evaluated as a substrate for a proline-directed protein kinase (p34cdc2/p58cyclin A) which recognizes the phosphorylation site motif X-Ser/Thr-Pro-X. The shortest human tau isoform, expressed as a recombinant protein, was phosphorylated to a stoichiometry of 2 mol phosphate/mol tau. Phosphoamino acid analysis revealed phosphorylation of both serine and threonine residues. Phosphorylation of recombinant tau resulted in a decreased ability to induce microtubule assembly but had no effect on the final extent of microtubule formation or on the rate of cold-induced microtubule disassembly. Phosphorylation of tau by the proline-directed protein kinase completely blocked immunoreactivity with antibody SMI33. Phosphorylation did not create the epitopes for the phosphate-dependent antibodies SMI31 or SMI34. Antibody SMI33 recognizes neurofibrillary tangles after treatment with alkaline phosphatase, suggesting that the proline-directed protein kinase may phosphorylate tau at sites that are phosphorylated in Alzheimer's disease. |
| Databáze: | OpenAIRE |
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