![]()
|
|
||||||||
J. Biol. Chem., Vol. 277, Issue 18, 15237-15240, May 3, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Neuronal Cdc2-like kinase (Nclk) plays an
important role in a variety of cellular processes, including neuronal
cell differentiation, apoptosis, neuron migration, and formation of
neuromuscular 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 the
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 a
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.
ACCELERATED PUBLICATION
Identification of a Neuronal Cdk5 Activator-binding Protein as
Cdk5 Inhibitor*
§,
,
,
, and
**
Department of Biochemistry, Hong Kong
University of Science and Technology, Clear Water Bay, Kowloon, Hong
Kong, China and the ¶ Department of Medical Biochemistry, Faculty
of Medicine, University of Calgary, Calgary,
Alberta T2N 1N4, Canada
*
This work was supported by a grant from the Research Grants
Council of Hong Kong and Hong Kong AoE of Molecular Neuroscience.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Current address: Inst. of Molecular and Cell Biology, 30 Medical Dr., Singapore 117609, Singapore.
**
To whom correspondence should be addressed. Tel.: 852-2358-8701;
Fax: 852-2358-1552; E-mail: jerwang@ust.hk.
This article has been cited by other articles:
![]() |
Z. Hou, Q. Li, L. He, H.-Y. Lim, X. Fu, N. S. Cheung, D. X. Qi, and R. Z. Qi Microtubule Association of the Neuronal p35 Activator of Cdk5 J. Biol. Chem., June 29, 2007; 282(26): 18666 - 18670. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. J. Scott, K. L. Mohlke, L. L. Bonnycastle, C. J. Willer, Y. Li, W. L. Duren, M. R. Erdos, H. M. Stringham, P. S. Chines, A. U. Jackson, et al. A Genome-Wide Association Study of Type 2 Diabetes in Finns Detects Multiple Susceptibility Variants Science, June 1, 2007; 316(5829): 1341 - 1345. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Bomeke, R. Pries, V. Korte, E. Scholz, B. Herzog, F. Schulze, and G. H. Braus Yeast Gcn4p Stabilization Is Initiated by the Dissociation of the Nuclear Pho85p/Pcl5p Complex Mol. Biol. Cell, July 1, 2006; 17(7): 2952 - 2962. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. C. B. Lim, Z. Hou, C.-P. Goh, and R. Z. Qi Protein Kinase CK2 Is an Inhibitor of the Neuronal Cdk5 Kinase J. Biol. Chem., November 5, 2004; 279(45): 46668 - 46673. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Druker, T. J. Bruxner, N. J. Lehrbach, and E. Whitelaw Complex patterns of transcription at the insertion site of a retrotransposon in the mouse Nucleic Acids Res., November 1, 2004; 32(19): 5800 - 5808. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |