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Originally published In Press as doi:10.1074/jbc.M909256199 on April 28, 2000

J. Biol. Chem., Vol. 275, Issue 30, 23139-23145, July 28, 2000
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Truncated Form of Importin alpha  Identified in Breast Cancer Cell Inhibits Nuclear Import of p53*

Il-Soo Kim, Dong-Hwan Kim, Su-Mi Han, Mi-Uk Chin, Hye-Jung Nam, Hyun-Pil Cho, Sang-Yong Choi, Byung-Joo Song, Eun-Ryoung Kim, Yong-Soo BaeDagger , and Young-Ho Moon§

From the Sung Ae Life Science Research Institute, Kyeonggi 423-030, South Korea and the Dagger  Department of Microbiology, Hannam University, Ojeong-dong 133, Daeduk-gu, Taejeon 306-791, South Korea

Disruption of the function of tumor suppressor proteins occasionally can be dependent on their subcellular localization. In about 40% of the breast cancer tissues, p53 is found in the cytoplasm as opposed to the nucleus, where it resides in normal breast cells. This means that the regulation of subcellular location of p53 is an important mechanism in controlling its function. The transport factors required for the nuclear export of p53 and the mechanisms of their nuclear export have been extensively characterized. However, little is known about the mechanism of nuclear import of p53. p53 contains putative nuclear localization signals (NLSs) which would interact with a nuclear transport factor, importin alpha . In this report we demonstrate that importin alpha  binds to NLSI in p53 and mediates the nuclear import of p53. Reverse transcriptase-polymerase chain reaction and sequencing analyses showed that a truncated importin alpha  deleted the region encoding the putative NLS-binding domain of p53, suggesting that it could not bind to NLSs of p53 proteins. Binding of importin alpha  to p53 was confirmed by using yeast two-hybrid assay. When expressed in CHO-K1 cells, the truncated importin alpha  predominantly localized to the cytoplasm. In truncated importin alpha  expressing cells, p53 preferentially localized to cytoplasmic sites as well. A significant increase in the p21waf1/cip1 mRNA level and induction of apoptosis were also observed in importin alpha  overexpressing cells. These results strongly suggest that importin alpha  functions as a component of the NLS receptor for p53 and mediates nuclear import of p53.

* This work was supported in part by Korea Research Foundation Grant 1998-019-F00034.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.

§ To whom correspondence should be addressed: 389 Chulsan, Kwangmyeong, Kyeonggi 423-030, Korea. Tel.: 82-2-6807-164/165; Fax: 82-2-6807-162; E-mail: hjyhdjsj@sungae.co.kr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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