[HTML][HTML] Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase* 210
NM Conus, KM Hannan, BE Cristiano… - Journal of Biological …, 2002 - ASBMB
Understanding the regulation of Akt has been of major interest for elucidating the control of
normal cellular physiology as well as malignant transformation. The paradigm for activation
of Akt involves phosphatidylinositol 3-kinase-dependent membrane localization followed by
activating phosphorylation of Thr-308 and Ser-473. Many of the activating signals for Akt
involve the stimulation of receptor and non-receptor tyrosine kinases, and the most potent
activator known is the tyrosine phosphatase inhibitor pervanadate, highlighting a possible …
normal cellular physiology as well as malignant transformation. The paradigm for activation
of Akt involves phosphatidylinositol 3-kinase-dependent membrane localization followed by
activating phosphorylation of Thr-308 and Ser-473. Many of the activating signals for Akt
involve the stimulation of receptor and non-receptor tyrosine kinases, and the most potent
activator known is the tyrosine phosphatase inhibitor pervanadate, highlighting a possible …
