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J. Biol. Chem., Vol. 280, Issue 24, 22937-22944, June 17, 2005

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Nuclear-Cytoplasmic Shuttling of a RING-IBR Protein RBCK1 and Its Functional Interaction with Nuclear Body Proteins^*

Kenji Tatematsu, Nobuo Yoshimoto, Tomoyoshi Koyanagi, Chiharu Tokunaga¶, Taro Tachibana||, Yoshihiro Yoneda||, Minoru Yoshida**, Toshihide Okajima, Katsuyuki Tanizawa, and Shun'ichi Kuroda

From the Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan, the ^¶Biosignal Research Center, Kobe University, Kobe, Hyogo 657-8501, Japan, the ^||Department of Cell Biology and Neuroscience, Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan, and the ^**Chemical Genetics Laboratory, RIKEN, Wako, Saitama 351-0198, Japan

The intracellular localization of a RING-IBR protein, RBCK1, possessing DNA binding and transcriptional activities, has been investigated. The endogenous RBCK1 was found in both the cytoplasm and nucleus. Particularly in the nucleus, it was localized in the granular structures, most likely nuclear bodies. In contrast, the over-expressed RBCK1 was detected exclusively in the cytoplasm. When the cells were treated with leptomycin B, the over-expressed RBCK1 accumulated in the nuclear bodies. These results suggest that RBCK1 possesses the signal sequences responsible for the nuclearcytoplasmic translocation. Mutational analysis of RBCK1 has indicated that an N-terminal region containing Leu-142 and Leu-145 and a C-terminal one containing the RING-IBR domain serve as the nuclear export and localization signals, respectively. Thus, RBCK1 is a transcription factor dynamically shuttling between cytoplasm and nucleus. Furthermore, RBCK1 was found to interact with nuclear body proteins, CREB-binding protein (CBP), and promyelocytic leukemia protein (PML). Coexpression of RBCK1 with CBP significantly enhanced the transcriptional activity of RBCK1. Although PML per se showed no effect on the transcriptional activity of RBCK1, the CBP-enhanced activity was repressed by coexpression with PML, presumably through the interaction of PML and CBP. Taken together, our data demonstrate that RBCK1 is involved in transcriptional machinery in the nuclear bodies, and its transcriptional activity is regulated by nucleocytoplasmic shuttling.

Received for publication, November 30, 2004 , and in revised form, April 14, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Dept. of Structural Molecular Biology, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan. Tel.: 81-6-6879-8461; Fax: 81-6-6879-8464; E-mail: kenji44{at}sanken.osaka-u.ac.jp.

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