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Distinct regulatory mechanism for p70 S6 kinase β from that for p70 S6 kinase α by Taichi Minami; Kenta Hara; Noriko Oshiro; Sachiko Ueoku; Ken‐ichi Yoshino; Chiharu Tokunaga; Yasuhito Shirai; Naoaki Saito; Ivan Gout; Kazuyoshi Yonezawa is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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**Background** A novel ribosomal S6 kinase, termed p70 S6 kinase β (p70β), has a highly homologous amino acid sequence to that of p70/p85 S6 kinase (p70α). This includes the critical phosphorylation sites, Thr^252^, Ser^394^ and Thr^412^ in p70α1, which correspond to Thr^241^, Ser^383^ and Thr^401^ in p70β1, respectively. However, the regulatory mechanism for p70β remains to be elucidated. **Results** We report here the expression and the mechanism of __in vivo__ regulation of p70β. Two isoforms, p70β1 and p70β2, were expressed in a variety of tissues at a different level. p70β1 was mainly targeted to the nucleus, whereas p70β2 dispersed throughout the cytoplasm including nucleoplasm. The kinase activity of p70β1 was less sensitive to the inhibition induced by rapamycin, wortmannin and amino acid withdrawal than that of p70α. The portion of p70β activity inhibited by rapamycin was rescued by the rapamycin‐resistant mutant of the mammalian target of rapamycin (mTOR). Mutational analysis revealed that the phosphorylation of Thr^241^ and Thr^401^ in p70β1 was indispensable for the kinase activity. In contrast, a p70β1 mutant in which Ser^383^ was substituted with Gly (S383G) still ret

Who reads Distinct regulatory mechanism for p70 S6 kinase β from that for p70 S6 kinase α?

Author

Taichi Minami; Kenta Hara; Noriko Oshiro; Sachiko Ueoku; Ken‐ichi Yoshino; Chiharu Tokunaga; Yasuhito Shirai; Naoaki Saito; Ivan Gout; Kazuyoshi Yonezawa

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 1356-9597)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)