A cdc2‐related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline‐directed protein kinase associated with microtubule
- 6 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 335 (2) , 171-175
- https://doi.org/10.1016/0014-5793(93)80723-8
Abstract
We previously reported that tau protein kinase II (TPKII) from bovine brain was composed of 30 kDa and 23 kDa subunits. The 30 kDa subunit of TPKII can be regarded as a catalytic subunit because of its ATP‐binding activity. Antibodies directed against TPKII‐phosphorylated tau also reacted with tau phosphorylated by cdc2 kinase obtained from starfish oocytes, indicating that TPKII and cdc2 kinase phosphorylate the same sites. We determined the amino acid sequence of the 30 kDa subunit and found it to be homologous with a cdc2‐related kinase, PSSALRE/cdk5. Moreover, an antibody against PSSALRE/cdk5 reacted with the 30 kDa subunit. These results indicate that the 30 kDa subunit of TPKII is bovine homologue of PSSALRE/cdk5. Expression of the 30 kDa subunit mRNA was enhanced in juvenile rat brain. This result supports our previous hypothesis that the kinase works actively in juvenile brain.Keywords
This publication has 39 references indexed in Scilit:
- Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filamentsFEBS Letters, 1993
- Brain Protein Kinase PK40erk Converts TAU into a PHF-like Form as Found in Alzheimer′s DiseaseBiochemical and Biophysical Research Communications, 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
- p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's diseaseFEBS Letters, 1992
- Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinaseNeuroscience Letters, 1992
- Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's diseaseFEBS Letters, 1992
- The Alzheimer‐like phosphorylation of tau protein reduces microtubule binding and involves Ser‐Pro and Thr‐Pro motifsFEBS Letters, 1992
- Fetal‐Type Phosphorylation of the τ in Paired Helical FilamentsJournal of Neurochemistry, 1992
- A novel brain‐specific 25 kDa protein (p25) is phosphorylated by a Ser/Thr‐Pro kinase (TPK II) from tau protein kinase fractionsFEBS Letters, 1991