Cyclic nucleotide- and Ca2+-independent phosphorylation of tubulin and microtubule-associated protein-2 by glycogen synthase (casein) kinase-1
| Autor: | Martin Flavin, Kuo-Ping Huang, Toolsee J. Singh, Adavi S. N. Murthy, Akira Akatsuka |
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| Rok vydání: | 1984 |
| Předmět: |
Biophysics
Biochemistry Substrate Specificity Cyclic nucleotide chemistry.chemical_compound Tubulin Casein kinase 2 alpha 1 Glycogen branching enzyme Cyclic AMP Animals Phosphorylation Protein kinase A Glycogen synthase Molecular Biology biology Chemistry Kinase Proteins Cell Biology Molecular biology Calcium-Calmodulin-Dependent Protein Kinases biology.protein Calcium Cattle Electrophoresis Polyacrylamide Gel Casein kinase 1 Microtubule-Associated Proteins Protein Kinases |
| Zdroj: | Biochemical and biophysical research communications. 121(1) |
| ISSN: | 0006-291X |
| Popis: | MAP-2 and tubulin are both shown to be substrates for glycogen synthase (casein) kinase-1 (CK-1). Greater than 40 mol 32P is incorporated into MAP-2 by CK-1 compared to only 14 mol 32P observed when cyclic AMP-dependent protein kinase (A-kinase) is the catalyst. Peptide mapping shows that CK-1 and A-kinase recognize a few common sites; the majority of the sites phosphorylated on MAP-2 by CK-1 are quite distinct. Up to 4 mol 32P can be incorporated into the tubulin dimer by CK-1 compared to only 0.9 mol 32P by A-kinase. The preferred substrate for both kinases is β-tubulin. |
| Databáze: | OpenAIRE |
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