Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M512663200
Title: Identification of nuclear import mechanisms for the neuronal Cdk5 activator
Authors: Fu, X.
Choi, Y.-K.
Qu, D.
Yu, Y.
Nam, S.C. 
Qi, R.Z.
Issue Date: 22-Dec-2006
Citation: Fu, X., Choi, Y.-K., Qu, D., Yu, Y., Nam, S.C., Qi, R.Z. (2006-12-22). Identification of nuclear import mechanisms for the neuronal Cdk5 activator. Journal of Biological Chemistry 281 (51) : 39014-39021. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M512663200
Abstract: 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-β, 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-β/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. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/107727
ISSN: 00219258
DOI: 10.1074/jbc.M512663200
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