PDK1 and cancer: AKT hyperactivation is associated with many pathophysiological conditions, including human cancers.[30] The phosphorylation of two key residues on AKT, including T308 regulated by the phosphoinositide‐dependent protein kinase 1 (PDK1) and S473 regulated by the mammalian target of rapamycin complex 2 (mTORC2), is indispensable for maximal activation of the kinase.[31] We here demonstrated that STK24 modulates IFN‐γ induced AKT1 activation via phosphorylating AKT1 at Thr21, a previously unrecognized phosphorylation site.