Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1

By A. Kim, G. Khursigara, Xuan Sun, T. Franke, M. Chao. Molecular and Cellular Biology, 2001

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AKT/PKB signaling: navigating downstream. (2007, positive): “Akt can directly phosphorylate the amino acid residue S83 on apoptosis signal-regulated kinase 1 (ASK1, also known as MAPKKK5), which is an upstream activating kinase within the JNK and p38 pathways (Kim et al., 2001).”
In brief (2011, neutral): “Both treatments induce cell death in an Akt-sensitive manner (He et al., 2010; Kim et al., 2001; Wang et al., 2000).”
Activation of the PI3K/Akt pathway and chemotherapeutic resistance. (2002, background): “Akt can also directly regulate the apoptotic machinery by phosphorylating and inactivating pro-apoptotic proteins such as BAD, which controls release of cytochrome c from mitochondria, and ASK1 (apoptosis signal-regulating kinase-1), a mitogen-activated protein kinase involved in stress- and cytokin”
PI3K/Akt: getting it right matters (2008, background): “It has been shown that apoptosis signal-regulating kinase 1 (ASK1) is regulated by Akt and contains an Akt-specific phosphorylation site (Kim et al., 2001).”
Redox Regulation of Cell Survival (2008, positive): “Furthermore, Akt also exerts its antiapoptotic function by phosphorylation and inhibition of ASK1 activity, which prevent stress-induced apoptosis (154).”