| First Author | Honda R | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 230 |
| Issue | 2 | Pages | 262-5 |
| PubMed ID | 9016762 | Mgi Jnum | J:37892 |
| Mgi Id | MGI:85287 | Doi | 10.1006/bbrc.1996.5933 |
| Citation | Honda R, et al. (1997) 14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase. Biochem Biophys Res Commun 230(2):262-5 |
| abstractText | To identify proteins which bind to mouse wee1 kinase, the yeast two-hybrid system was used with a mouse cDNA library. Using the carboxyl half of weel kinase, the 14-3-3 zeta protein was isolated. Recombinant 14-3-3 zeta was demonstrated to bind to wee1 kinase in vitro. The wee1 kinase phosphorylated by cdc2 kinase also bound to 14-3-3 zeta protein. When both wee1 kinase and 14-3-3 zeta were transfected into COS-1 cells, they formed a complex in a cell. The sequence of wee1 kinase necessary for the binding was tested by a two hybrid system expressing different lengths of peptides derived from wee1 kinase. Both the entire kinase domain and a sequence in the carboxyl terminus was thought to be necessary for the binding. The function of 14-3-3 zeta protein remained to be elucidated in relation to the regulation of G2 to M phase transition through wee1 kinase. |
