[HTML][HTML] Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization
N Fujita, S Sato, T Tsuruo - Journal of Biological Chemistry, 2003 - ASBMB
The cyclin-dependent kinase inhibitor p27 Kip1 plays an important role in cell cycle
regulation. The cyclin-dependent kinase-inhibitory activity of p27 Kip1 is regulated by
changes in its concentration and its subcellular localization. Several reports suggest that
phosphorylation of p27 Kip1 at serine 10, threonine 157, and threonine 187 regulate its
localization. We have previously identified that carboxyl-terminal threonine 198 (Thr 198) in
p27 Kip1 is a novel phosphorylation site and that Akt is associated with the phosphorylation …
regulation. The cyclin-dependent kinase-inhibitory activity of p27 Kip1 is regulated by
changes in its concentration and its subcellular localization. Several reports suggest that
phosphorylation of p27 Kip1 at serine 10, threonine 157, and threonine 187 regulate its
localization. We have previously identified that carboxyl-terminal threonine 198 (Thr 198) in
p27 Kip1 is a novel phosphorylation site and that Akt is associated with the phosphorylation …