Modulation of GSK‐3‐catalyzed phosphorylation of microtubule‐associated protein tau by non‐proline‐dependent protein kinases
Open Access
- 16 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 358 (1) , 4-8
- https://doi.org/10.1016/0014-5793(94)01383-c
Abstract
The phosphorylation of bovine tau, either by GSK‐3 alone or by a combination of GSK‐3 and several non‐proline‐dependent protein kinases (non‐PDPKs), was studied. GSK‐3 alone catalyzed the incorporation of ∼ 3 mol 32P/mot tau at a relatively slow rate. Prephosphorylation of tau by A‐kinase, C‐kinase, or CK‐2 (but not by CK‐1, CaM kinase II or Gr kinase) increased both the rate and extent of a subsequent phosphorylation catalyzed by GSK‐3 by several‐fold. These results suggest that the phosphorylation of tau by PDPKs such as GSK‐3 (and possibly MAP kinase, cdk5) may be positively modulated at the substrate level by non‐PDPK‐catalyzed phosphorylations.Keywords
This publication has 24 references indexed in Scilit:
- Abnormal Alzheimer‐like phosphorylation of tau‐protein by cyclin‐dependent kinases cdk2 and cdk5Published by Wiley ,1993
- Protein Kinase FA/GSK‐3 Phosphorylates on Ser235‐Pro and Ser404‐Pro that Are Abnormally Phosphorylated in Alzheimer's Disease BrainJournal of Neurochemistry, 1993
- Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filamentsFEBS Letters, 1993
- τ Protein Kinase II Is Involved in the Regulation of the Normal Phosphorylation State of τ ProteinJournal of Neurochemistry, 1993
- Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tauFEBS Letters, 1992
- Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filamentsNeuroscience Letters, 1992
- Phosphoserine as a recognition determinant for glycogen synthase kinase-3: Phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1Archives of Biochemistry and Biophysics, 1988
- Protein kinase C phosphorylates tau and induces its functional alterationsFEBS Letters, 1987
- Multisite phosphorylation of glycogen synthase from rabbit skeletal muscleFEBS Letters, 1982
- Phosphorylation of the Type‐II Regulatory Subunit of Cyclic‐AMP‐Dependent Protein Kinase by Glycogen Synthase Kinase 3 and Glycogen Synthase Kinase 5European Journal of Biochemistry, 1982