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. Author manuscript; available in PMC: 2022 Apr 1.
Published in final edited form as: Structure. 2020 Dec 3;29(4):320–329.e4. doi: 10.1016/j.str.2020.11.011

Figure 5. A model of RIAM activation by FAK and Src kinases.

Figure 5.

Dormant RIAM adopts an autoinhibited configuration with intermolecular interactions mediated by the PH domain and the N-terminal region. This autoinhibited configuration is released upon phosphorylation by FAK and Src kinases. FAK kinase phosphorylates the IN segment, unmasking the RAP1-binding site in the RA domain. Src kinase phosphorylates of the PH domain, unmasking the phosphoinositide-binding site in the PH domain. The two activating mechanisms of RA-PH by phosphorylation cooperatively activate RIAM, promoting the PM translocation of RIAM by interacting with RAP1 and PIP2.