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Ack1 Mediated AKT/PKB Tyrosine 176 Phosphorylation Regulates Its Activation
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Journal Article
Ack1 Mediated AKT/PKB Tyrosine 176 Phosphorylation Regulates Its Activation
2010
Overview
The AKT/PKB kinase is a key signaling component of one of the most frequently activated pathways in cancer and is a major target of cancer drug development. Most studies have focused on its activation by Receptor Tyrosine Kinase (RTK) mediated Phosphatidylinositol-3-OH kinase (PI3K) activation or loss of Phosphatase and Tensin homolog (PTEN). We have uncovered that growth factors binding to RTKs lead to activation of a non-receptor tyrosine kinase, Ack1 (also known as ACK or TNK2), which directly phosphorylates AKT at an evolutionarily conserved tyrosine 176 in the kinase domain. Tyr176-phosphorylated AKT localizes to the plasma membrane and promotes Thr308/Ser473-phosphorylation leading to AKT activation. Mice expressing activated Ack1 specifically in the prostate exhibit AKT Tyr176-phosphorylation and develop murine prostatic intraepithelial neoplasia (mPINs). Further, expression levels of Tyr176-phosphorylated-AKT and Tyr284-phosphorylated-Ack1 were positively correlated with the severity of disease progression, and inversely correlated with the survival of breast cancer patients. Thus, RTK/Ack1/AKT pathway provides a novel target for drug discovery.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
1-Phosphatidylinositol 3-kinase
/ Acids
/ Animals
/ Breast Neoplasms - pathology
/ Cancer
/ Female
/ Homology
/ Humans
/ Kinases
/ Male
/ Mice
/ Mutation
/ Pathology/Molecular Pathology
/ Phenols (Class of compounds)
/ Plasma
/ Prostate
/ Prostatic intraepithelial neoplasia
/ Prostatic Intraepithelial Neoplasia - pathology
/ Protein-tyrosine kinase receptors
/ Protein-Tyrosine Kinases - metabolism
/ Protein-tyrosine-phosphatase
/ Proteins
/ Proto-Oncogene Proteins c-akt - metabolism
/ Tensin
/ Tumors
/ Tyrosine
