Identification of nuclear import mechanisms for the neuronal CDK5 activator

doi:10.1074/jbc.M512663200

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Papers In Press, published online ahead of print October 23, 2006
J. Biol. Chem, 10.1074/jbc.M512663200
Submitted on November 28, 2005
Revised on September 5, 2006
Accepted on October 23, 2006

Identification of nuclear import mechanisms for the neuronal CDK5 activator

Xinrong Fu, Yuk-Kwan Choi, Dianbo Qu, Yan Yu, Nam Sang Cheung, and Robert Z. Qi

Biochemistry, Hong Kong University of Science and Technology, Hong Kong

Corresponding Author: qirz{at}ust.hk

The activation of Cdk5 by p35 plays a pivotal role in a multitude of nervous system activities ranging from neuronal differentiation to degeneration. A fraction of Cdk5 and p35 localizes in the nucleus where Cdk5-p35 exerts its functions via protein phosphorylation, and p35 displays a dynamic localization between the cytoplasm and the nucleus. Here, we examined the nuclear import properties of p35. In nuclear import assays, p35 was actively transported into the nuclei of digitonin-permeabilized HeLa cells and cortical neurons by cytoplasmic carrier-mediated mechanisms. Importin-ß, importin-5, and importin-7 were identified to import p35 into the nuclei via a direct interaction with it. An N-terminal region of p35 was defined to interact with the above importins, serving as a nuclear localization signal. Finally, we show that the nuclear localization of p35 does not require the association of Cdk5. Furthermore, Cdk5 and importin-ß/5/7 are mutually exclusive in binding to p35. These results suggest that p35 employs pathways distinct from that used by Cdk5 for transport to the nucleus.

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