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Annals of Oncology Advance Access originally published online on May 13, 2008
Annals of Oncology 2008 19(7):1356-1357; doi:10.1093/annonc/mdn293
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© The Author 2008. Published by Oxford University Press on behalf of the European Society for Medical Oncology. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

letters to the editor

Insulin receptor substrate protein 53 (IRSp53) as a binding partner of antimetastasis molecule NESH, a member of Abelson interactor protein family

The first 10% of the full text of this article appears below.

Involvement of NESH in cancer invasion and metastasis is now very important and interesting. In order to clarify the molecular mechanisms, we identified insulin receptor substrate protein 53 (IRSp53) as a partner of NESH utilizing a conventional yeast two-hybrid screen with a proline-rich domain of NESH as bait. The specific interaction was confirmed by coimmunoprecipitation assay and colocalization analysis in mammalian cells. The carboxyl-terminal SH3 domain of IRSp53 is responsible for the interaction with the proline-rich domain of NESH. NESH may play a critical role in regulating the actin cytoskeleton required . . . [Full Text of this Article]

funding

S. Matsuda1,2,{dagger}, S. Yokozaki2,3,{dagger}, H. Yoshida1, Y. Kitagishi1, N. Shirafuji4 and N. Okumura1

1 Department of Environmental Health, Nara Women's University, Nara 630-8506
2 Department of Molecular Pathogenesis
3 Second Department of Internal Medicine, Nagoya University School of Medicine, Nagoya 466-8550
4 Department of Hematology/Oncology, Teikyo University School of Medicine, Tokyo, Japan

* (E-mail: smatsuda@cc.nara-wu.ac.jp)


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