@article{oai:kanazawa-u.repo.nii.ac.jp:00015309,
 author = {Uchida, Sanae and Kubo, Akitsugu and Kizu, Ryoichi and Nakagama, Hitoshi and Matsunaga, Tsukasa and Ishizaka, Yukihito and Yamashita, Katsumi},
 issue = {4},
 journal = {Journal of Biochemistry},
 month = {Apr},
 note = {The phospho-site adapter protein 14-3-3 binds to target proteins at amino acid sequences matching the consensus motif Arg-X-X-Ser/Thr-X-Pro, where the serine or threonine residue is phosphorylated and X is any amino acid. The dual-specificity phosphatase CDC25B, which is involved in cell cycle regulation, contains five 14-3-3 binding motifs, but 14-3-3 preferentially binds to the motif at Ser309 in CDC25B1 (or Ser323 in CDC25B3). In the present study, we demonstrate that amino acid residues C-terminal to the 14-3-3 binding motif strongly affect the efficiency of 14-3-3 binding. Alanine substitutions at residues downstream of the Ser309 motif dramatically reduced 14-3-3 binding, although phosphorylation of Ser309 was unaffected. We also observed that binding of endogenous 14-3-3 to mutant CDC25B occurred less efficiently than to the wild type. Mutants to which 14-3-3 cannot bind efficiently tend to be located in the nucleus, although not as specifically as the alanine substitution mutant of Ser309. These results indicate that amino acid sequences C-terminal to the consensus binding site have an important role in the efficient binding of 14-3-3 to at least CDC25B, which may partly explain why some consensus sequences are inactive as 14-3-3 binding sites. © 2006 The Japanese Biochemical Society., 金沢大学医薬保健研究域薬学系},
 pages = {761--769},
 title = {Amino acids C-terminal to the 14-3-3 binding motif in CDC25B affect the efficiency of 14-3-3 binding},
 volume = {139},
 year = {2006}
}