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First published online 1 June 2004
doi: 10.1242/jcs.01086

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Binding of 14-3-3ß but not 14-3-3 controls the cytoplasmic localization of CDC25B: binding site preferences of 14-3-3 subtypes and the subcellular localization of CDC25B

Sanae Uchida¹, Akiko Kuma^1,*, Motoaki Ohtsubo², Mari Shimura³, Masato Hirata⁴, Hitoshi Nakagama⁵, Tsukasa Matsunaga⁶, Yukihito Ishizaka³ and Katsumi Yamashita^1,

¹ Division of Life Science, Graduate School of Natural Science and Technology, Kanazawa University, Kakuma-machi, Kanazawa, 920-1192, Japan
² Institute of Life Science, Kurume University, Aikawa 2432-3, Kurume, 839-0861, Japan
³ Division of Intractable Disease, International Medical Center of Japan, 21-1 Toyama 1-chome, Shinjuku-ku, Tokyo, 162-8655, Japan
⁴ Laboratory of Molecular and Cellular Biochemistry, Faculty of Dental Science, and Station for Collaborative Research, Kyushu University, Maidashi, Fukuoka, 812-8582, Japan
⁵ Biochemistry Division, National Cancer Center Research Institute, 1-1 Tsukiji 5-chome, Chuo-ku, Tokyo, 104-0045, Japan
⁶ Laboratory of Molecular Human Genetics, Faculty of Pharmaceutical Sciences, Kanazawa University, 13-1 Takara-machi, Kanazawa, 920-0934, Japan

Author for correspondence (e-mail: katsumi{at}kenroku.kanazawa-u.ac.jp)

Accepted 7 January 2004

The dual specificity phosphatase CDC25B positively controls the G2-M transition by activating CDK1/cyclin B. The binding of 14-3-3 to CDC25B has been shown to regulate the subcellular redistribution of CDC25B from the nucleus to the cytoplasm and may be correlated with the G2 checkpoint. We used a FLAG-tagged version of CDC25B to study the differences among the binding sites for the 14-3-3 subtypes, 14-3-3ß, 14-3-3 and 14-3-3, and the relationship between subtype binding and the subcellular localization of CDC25B. All three subtypes were found to bind to CDC25B. Site-directed mutagenesis studies revealed that 14-3-3ß bound exclusively near serine-309 of CDC25B1, which is within a potential consensus motif for 14-3-3 binding. By contrast, 14-3-3 bound preferentially to a site around serine-216, and the presence of serine-137 and -309 enhanced the binding. In addition to these binding-site differences, we found that the binding of 14-3-3ß drove CDC25B to the cytoplasm and that mutation of serine-309 to alanine completely abolished the cytoplasmic localization of CDC25B. However, co-expression of 14-3-3 and CDC25B did not affect the subcellular localization of CDC25B. Furthermore, serine-309 of CDC25B was sufficient to produce its cytoplasmic distribution with co-expression of 14-3-3ß, even when other putative 14-3-3 binding sites were mutated. 14-3-3 resembled 14-3-3ß with regard to its binding to CDC25B and the control of CDC25B subcellular localization. The results of the present study indicate that two 14-3-3 subtypes can control the subcellular localization of CDC25B by binding to a specific site and that 14-3-3 has effects on CDC25B other than the control of its subcellular localization.

Key words: CDC25B, 14-3-3ß, 14-3-3, Subcellular localization, G2 checkpoint

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