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A more recent version of this article appeared on September 10, 2004
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M401663200v1
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Papers In Press, published online ahead of print June 18, 2004
J. Biol. Chem, 10.1074/jbc.M401663200
Submitted on February 15, 2004
Revised on June 17, 2004
Accepted on June 18, 2004

Nucleocytoplasmic shuttling of RIP3: Identification of novel nuclear export and import signals in RIP3

Yonghui Yang, Jun Ma, Youjun Chen, and Mian Wu

Department of Molecular and Cell Biology, University of Science and Technology of China, Hefei, Anhui 230026

Corresponding Author: wumian88{at}yahoo.com

Receptor-interacting protein 3 (RIP3), a member of the RIP Ser/Thr kinase family, has been characterized as a pro-apoptotic protein involved in TNFR1 signaling pathway. In this study, we have mapped a minimal region of RIP3 sufficient for apoptosis induction to a fragment of thirty-one amino acids in length. This minimal region also functions as an unconventional nuclear localization signal (NLS) sufficient to confer the import of full-length RIP3 to the nucleus to trigger apoptosis, suggesting that RIP3 is able to play an apoptosis-inducing role in the nucleus. In addition, we have characterized two novel leucine-rich nuclear export signals (NESs), which are responsible for the nuclear export of RIP3 to the cytoplasm via a CRM1-dependent pathway, and an extra leucine-rich NES in the N-terminus of RIP3, which contributes to the cytoplasmic distribution in a CRM1-independent manner. Thus, we provide the first evidence that RIP3 acts a nucleocytoplasmic shuttling protein, which presents a possible link between death receptor signaling and nuclear apoptosis.


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