702-Structural Basis for mTORC2 & Akt Phosphorylation

Paper Talk · Mar 27, 2026 · 16m

This research article identifies the structural basis for how the protein kinase mTORC2 selectively recruits and phosphorylates Akt and related AGC family kinases. Researchers utilized expressed protein ligation to create semisynthetic Akt probes, allowing them to trap the transient kinase-substrate interaction for high-resolution cryo-electron microscopy analysis. The study reveals that mTORC2 recognition depends on two distinct long-range docking interfaces—the CRIM domain and the "N-mooring" of the mSin1 subunit—rather than the local amino acid sequence surrounding the phosphorylation…