Differential cellular phosphorylation of neurofilament heavy side-arms by glycogen synthase kinase-3 and cyclin-dependent kinase-5
| Autor: | Sonia Guidato, James R. Woodgett, Christopher C.J. Miller, Li-Huei Tsai |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Central Nervous System
Neurofilament macromolecular substances Protein Serine-Threonine Kinases Biochemistry Cell Line Cellular and Molecular Neuroscience Glycogen Synthase Kinase 3 GSK-3 Neurofilament Proteins Peripheral Nervous System Animals Phosphorylation Glycogen synthase Protein kinase A biology Kinase Activator (genetics) Cyclin-dependent kinase 5 Glycogen Synthase Kinases Cyclin-Dependent Kinase 5 Molecular biology Cyclin-Dependent Kinases Rats Calcium-Calmodulin-Dependent Protein Kinases biology.protein Microtubule-Associated Proteins |
| Zdroj: | Journal of neurochemistry. 66(4) |
| ISSN: | 0022-3042 |
| Popis: | To investigate the cellular mechanisms regulating neurofilament-heavy subunit (NF-H) side-arm phosphorylation, we studied the ability of three putative neurofilament kinases, glycogen synthase kinase-3 (GSK-3)alpha, GSK-3 beta, and cyclin-dependent kinase-5 (cdk-5), to phosphorylate NF-H in transfected cells. We analysed NF-H phosphorylation by using a panel of phosphorylation-dependent antibodies and also by monitoring the electrophoretic mobility of the transfected NF-H on sodium dodecyl sulphate-polyacrylamide gel electrophoresis because this is known to be affected by side-arm phosphorylation. Our results demonstrate that whereas GSK-3 alpha, GSK-3 beta, and cdk-5 will all phosphorylate NF-H, they generate different antibody reactivity profiles. GSK-3 alpha and GSK-3 beta induce a partial retardation of a proportion of the transfected NF-H, but only cdk-5 alters the rate of electrophoretic migration to that of NF-H from brain. We conclude that cdk-5 and GSK-3 phosphorylate different residues or sets of residues within NF-H sidearm in cells. We further show that cdk-5 is active in both the CNS and the PNS but that this activity is not dependent on expression of its activator, p35. This suggests that there are other activators of cdk-5. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text