A brain-specific activator of cyclin-dependent kinase 5.

Nature 1994 Sep;371(6496):423-6

MRC Group in Signal Transduction, University of Calgary, Alberta, Canada.

Phosphorylation of the neurofilament proteins of high and medium relative molecular mass, as well as of the Alzheimer's tau protein, is thought to be catalysed by a protein kinase with Cdc2-like substrate specificity. We have purified a novel Cdc2-like kinase from bovine brain capable of phosphorylating both the neurofilament proteins and tau. The purified enzyme is a heterodimer of cyclin-dependent kinase 5 (Cdk5) and a novel regulatory subunit, p25 (ref. 8). When overexpressed and purified from Escherichia coli, p25 can activate Cdk5 in vitro. Unlike Cdk5, which is ubiquitously expressed in human tissue, the p25 transcript is expressed only in brain. A full-length complementary DNA clone showed that p25 is a truncated form of a larger protein precursor, p35, which seems to be the predominant form of the protein in crude brain extract. Cdk5/p35 is the first example of a Cdc2-like kinase with neuronal function.

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http://dx.doi.org/10.1038/371423a0DOI Listing
September 1994

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References

(Supplied by CrossRef)

M Hasegawa et al.
J. biol. Chem. 1992

ZS Xu et al.
J. biol. Chem. 1992

VM Lee et al.
Proc. natn. Acad. Sci. U.S.A 1988

M Mawal-Dewan et al.
J. biol. Chem. 1992

R Vulliet et al.
J. biol. chem. 1992

S Hisanaga et al.
J. biol. Chem. 1991

RG Guan et al.
J. Neurochem. 1992

J Lew et al.
J. biol. Chem. 1992

J Lew et al.
J. biol. Chem. 1992

H Paudel et al.
J. biol. Chem. 1993

M Meyerson et al.
EMBO J. 1992

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