MULAN Akt
Cell Research , (13 March 2012) | doi:10.1038/cr.2012.38
Akt is negatively regulated by the MULAN E3 ligase
Seunghee Bae, Sun-Yong Kim, Jin Hyuk Jung, Yeongmin Yoon, Hwa Jun Cha, Hyunjin Lee, Karam Kim, Jongran Kim, In-Sook An, Jongdoo Kim, Hong-Duck Um, In-Chul Park, Su-Jae Lee, Seon Young Nam, Young-Woo Jin, Jae Ho Lee and Sungkwan An
Abstract
The serine/threonine kinase Akt functions in multiple cellular processes, including cell survival and tumor development. Studies of the mechanisms that negatively regulate Akt have focused on dephosphorylation-mediated inactivation. In this study, we identified a negative regulator of Akt, MULAN, which possesses both a RING finger domain and E3 ubiquitin ligase activity. Akt was found to directly interact with MULAN and to be ubiquitinated by MULAN in vitro and in vivo. Other molecular assays demonstrated that phosphorylated Akt is a substantive target for both interaction with MULAN and ubiquitination by MULAN. The results of the functional studies suggest that the degradation of Akt by MULAN suppresses cell proliferation and viability. These data provide insight into the Akt ubiquitination signaling network.
最終更新:2012年03月19日 13:33