The serine/threonine kinase Akt also known as protein kinase B (PKB) or Rac, plays a crucial role in controlling many diverse and important cellular functions such as cell survival and glycogen metabolism (Hajduch et al., 2001 and Nicholson & Anderson, 2002). Three isoforms (alpha, beta, and gamma) have been identified that can be activated rapidly in response to insulin and growth factors in a phosphoinositide 3-kinase (PI3K)-dependent fashion (Hajduch et al., 2003). Phosphorylation of Aktalpha occurs at two specific regulatory sites in Drosophila, one localized in the kinase domain, Thr342, and the other in the C-terminal regulatory domain, Ser505: these two activation sites are homologous to mammalian Ser473 and Thr308 respectively (Powell et al., 2004).
The serine/threonine kinase Akt also known as protein kinase B (PKB) or Rac, plays a crucial role in controlling many diverse and important cellular functions such as cell survival and glycogen metabolism (Hajduch et al., 2001 and Nicholson & Anderson
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