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Figure 1 | Cell Division

Figure 1

From: Akt finds its new path to regulate cell cycle through modulating Skp2 activity and its destruction by APC/Cdh1

Figure 1

Schematic model for how Akt1-dependent phosphorylation of Skp2 at the Ser72 site promotes Skp2 cytoplasmic localization and stabilizes Skp2 by impairing its association with the APC/Cdh1 E3 ubiquitin ligase complex. Phosphorylation of Skp2 at Ser72 by Akt1 greatly reduces its ability to interact with the importin complex as well as promotes its association with 14-3-3, resulting in cytoplasmic retention. Furthermore, phosphorylation of Skp2 by Akt1 primes Skp2 for subsequent phosphorylation of Ser75 by Casein Kinase I (CKI). Phosphorylation on both Ser72 and Ser75 results in impaired association with Cdh1, thus allowing Skp2 to escape APC/Cdh1-mediated ubiquitination and destruction.

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