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A more recent version of this article appeared on May 3, 2002
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C200032200v1
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Papers In Press, published online ahead of print March 6, 2002
J. Biol. Chem, 10.1074/jbc.C200032200
Submitted on January 16, 2002
Revised on February 25, 2002
Accepted on March 6, 2002

Identification of a neuronal Cdk5 activator-binding protein as Cdk5 inhibitor

Yick-Pang Ching, Andy S.H. Pang, Wing-Ho Lam, Robert Z. Qi, and Jerry H. Wang

Biochemistry, Hong Kong University os Science and Technology, Kowloon, Hongkong

Corresponding Author: jerwang{at}ust.hk

Neuronal cdc2-like kinase (Nclk) plays an important role in a variety of cellular processes, including neuronal cell differentiation, apoptosis, neuron migration and neuro-muscular junction. The active kinase consists of a catalytic subunit, Cdk5, and an essential regulatory subunit, neuronal Cdk5 Activator (p35nck5a or p25nck5a), which is expressed primarily in neurons of central nervous tissue. In our previous study using yeast two-hybrid screening method, three novel p35nck5a-associated proteins were isolated. Here we show that one of these proteins, called C42, specifically inhibits the activation of Cdk5 by Nck5a. Co-immunoprecipitation data suggested that C42 and p35nck5a could form complex within cultured mammalian cells. Deletion analysis has mapped the inhibitory domain of C42 to a region of 135 amino acids, which is conserved in Pho81, a yeast protein that inhibits the yeast cyclin-dependent protein kinase Pho85. The Pho85/Pho80 kinase complex has been shown to be the yeast functional homologue of the mammalian Cdk5/p35nck5a kinase.


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