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

@article{Kobayashi1993ACK,
  title={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},
  author={S. Kobayashi and Koichi Ishiguro and Akira Omori and Masako Takamatsu and Manabu Arioka and Kazutomo Imahori and Tsuneko Uchida},
  journal={FEBS Letters},
  year={1993},
  volume={335}
}
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… 
Precursor of cdk5 activator, the 23 kDa subunit of tau protein kinase II: Its sequence and developmental change in brain
TLDR
Findings suggest that p23 results from the processing of the precursor protein, pre‐p23, suggesting that its expression controls the phosphorylation of tau by the TPKII/TPKI system in the neonatal brain.
Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain
TLDR
It is suggested that the 23 kDa subunit, but not cyclin, activates cdk5 in neuronal cells, which no longer exhibit cell cycling but are terminally differentiated cells.
Porcine brain neurofilament-H tail domain kinase: its identification as cdk5/p26 complex and comparison with cdc2/cyclin B kinase.
TLDR
Using dephosphorylated neurofilament (NF) proteins as substrates, the kinase with a higher activity for the deph phosphorus-H than the phosphorylated form of NF-H was searched for in the porcine brain extract and did not display M-phase promoting activity when assayed with a cell-free system of Xenopus egg extract.
Inhibition of Protein Phosphatase 2A Overrides Tau Protein Kinase I/Glycogen Synthase Kinase 3β and Cyclin-dependent Kinase 5 Inhibition and Results in Tau Hyperphosphorylation in the Hippocampus of Starved Mouse*
TLDR
The results demonstrate that the activation of TPKI/GSK3β and cdk5 is not necessary to obtain hyperphosphorylated tau in vivo, and indicate that inhibition of PP2A is likely the dominant factor in inducing tau hyperph phosphorylation in the starved mouse, overriding the inhibition of key tau kinases.
Site-specific Phosphorylation of Synapsin I by Mitogen-activated Protein Kinase and Cdk5 and Its Effects on Physiological Functions*
TLDR
The results raise the possibility that the so-called proline-directed protein kinases together with CaM kinase II and cAMP-dependent protein kinase play an important role in the regulation of synapsin I function.
The protein kinase Cdk5
TLDR
The links between the studies on the Cdk5/p35 system in normal neurogenesis and its claimed participation in neurodegeneration, provide the framework to understand the regulatory relevance of this kinase system, and changes in its regulation that may be implicated in disturbances such as those occurring in Alzheimer disease.
Cdk5 and MAPK are associated with complexes of cytoskeletal proteins in rat brain.
TLDR
It is suggested that in mammalian brain, different kinases, their regulators and phosphatases form multimeric complexes with cytoskeletal proteins and regulate multisite phosphorylation from synthesis in the cell body to transport and assembly in the axon.
Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38δ at Thr50 promotes microtubule assembly
TLDR
A role for Tau in the adaptative response of neurons to stress is suggested and it is indicated that SAPK4/p38δ and/or SAPK3/p 38δ may contribute to the hyperphosphorylation of Tau inThe human tauopathies.
Stress‐Activated Protein Kinase/c‐Jun N‐Terminal Kinase Phosphorylates τ Protein
TLDR
It is shown that purified recombinant stress‐activated protein kinase/c‐Jun N‐terminal kinase, a proline‐directed kinase of the MAP kinase extended family, phosphorylates recombinant τ in vitro on threonine and serine residues.
Phosphorylation of microtubule‐associated protein tau by isoforms of c‐Jun N‐terminal kinase (JNK)
TLDR
It is shown that c‐Jun N‐terminal kinases JNK1, JNK2 and JNK3 phosphorylate tau at many serine/threonine–prolines, as assessed by the generation of the epitopes of phosphorylation‐dependent anti‐tau antibodies.
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Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments.
TLDR
TPKI was more effective than TPKII for producing the decrease of tau-1 immunoreactivity and mobility shift of t Tau on SDS-PAGE, and findings suggested that tau phosphorylated by TPKI resembled A-68, a component of paired helical filaments.
Tau protein kinase II has a similar characteristic to cdc2 kinase for phosphorylating neurofilament proteins.
TLDR
Tau protein kinase II purified from a bovine brain tau protein fraction was shown to have a similar substrate specificity to cdc2 kinase in that both phosphorylate neurofilament (NF) proteins.
Brain proline-directed protein kinase is a neurofilament kinase which displays high sequence homology to p34cdc2.
TLDR
The results suggest that the brain kinase represents a new category of the cdc2 family, and that some members of thecdc2 kinase family may have major functions unrelated to cell cycle control.
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TLDR
It is proposed that MAP kinase is abnormally active in Alzheimer brain tissue, or that the corresponding phosphatases are abnormally passive, due to a breakdown of the normal regulatory mechanisms.
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TLDR
It is suggested that τ protein kinase II is indirectly involved, at least in part, in the regulation of the phosphorylation state of τ in neuronal cells.
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TLDR
Results suggest a role for cdc2 and MAP2 kinases in phosphorylating tau protein at the tau‐1 epitope in Alzheimer's disease.
Phosphorylation of neurofilament H subunit at the tail domain by CDC2 kinase dissociates the association to microtubules.
We sought the mammalian neurofilament tail domain-specific kinase. Several well known kinases including cAMP-dependent protein kinase, protein kinase C, Ca(2+)-calmodulin-dependent protein kinase II,
Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
TLDR
Results suggested that TPKI might be responsible for at least some of the phosphorylation of tau to induce PHF formation.
A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope
TLDR
The kinase fraction contains a protein kinase activity recognizing serine/threonine proline sequence and phosphorylated tau at the tau-1 site previously reported as one of the phosphorylation sites on PHF by other groups.
A novel brain‐specific 25 kDa protein (p25) is phosphorylated by a Ser/Thr‐Pro kinase (TPK II) from tau protein kinase fractions
TLDR
Using immunoblot analysis, the novel brain‐specific 25 kDa protein was found only in brain extracts, and was most abundant in the brain regions such as cerebrum and hippocampus, but less abundant in cerebellum, medulla oblongata and olfactory bulb.
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