Small molecule-induced cytosolic activation of protein kinase Akt rescues ischemia-elicited neuronal death

Hakryul Jo(Boston Children's Hospital), Subhanjan Mondal(Boston Children's Hospital), Dewar J. Tan(Boston Children's Hospital), Eiichiro Nagata(Tokai University), Shunya Takizawa(Tokai University), Alok K. Sharma(Beth Israel Deaconess Medical Center), Qingming Hou(Boston University), Kumaran Shanmugasundaram(Beth Israel Deaconess Medical Center), Amit Prasad(Boston Children's Hospital), Joe K. Tung(Boston Children's Hospital), Alexander O. Tejeda(Boston Children's Hospital), Heng‐Ye Man(Boston University), Alan C. Rigby(Beth Israel Deaconess Medical Center), Hongbo R. Luo(Boston Children's Hospital)
Proceedings of the National Academy of Sciences
June 11, 2012
Cited by 368Open Access
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Abstract

Elevating Akt activation is an obvious clinical strategy to prevent progressive neuronal death in neurological diseases. However, this endeavor has been hindered because of the lack of specific Akt activators. Here, from a cell-based high-throughput chemical genetic screening, we identified a small molecule SC79 that inhibits Akt membrane translocation, but paradoxically activates Akt in the cytosol. SC79 specifically binds to the PH domain of Akt. SC79-bound Akt adopts a conformation favorable for phosphorylation by upstream protein kinases. In a hippocampal neuronal culture system and a mouse model for ischemic stroke, the cytosolic activation of Akt by SC79 is sufficient to recapitulate the primary cellular function of Akt signaling, resulting in augmented neuronal survival. Thus, SC79 is a unique specific Akt activator that may be used to enhance Akt activity in various physiological and pathological conditions.


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