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. Author manuscript; available in PMC: 2019 Apr 15.
Published in final edited form as: J Phys Chem B. 2018 Aug 8;122(49):11137–11146. doi: 10.1021/acs.jpcb.8b05982

Figure 8.

Figure 8.

Schematic illustration for CaM-driven PI3Kα activation. CaM shifts the equilibrium of the nSH2 and cSH2 domains, making their CaM-binding motifs change into α-helical conformations (nSH2α and cSH2α). Then, CaM forms strong interactions with both nSH2α and cSH2α to activate PI3Kα. CaM binds to and releases the nSH2 domain to allosterically activate PI3Kα, and the CaM interaction with the cSH2 domain facilitates PI3Kα membrane localization by binding of the other lobe of CaM to K-Ras4B on the membrane. Activated PI3Kα phosphorylates PIP2 to PIP3.