Commentary Open Access
Volume 2 | Issue 2 | DOI: https://doi.org/10.33696/Signaling.2.041

Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling

  • 1Molecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA
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Corresponding Author

Jinhua Wu, Jinhua.Wu@fccc.edu

Received Date: April 28, 2021

Accepted Date: May 27, 2021


Integrins are cellular receptors that regulate cell adhesion and many other cellular functions. Integrins can be activated via an “insideout pathway” that is promoted by RAP1 GTPase. RAP1-GTP-Interacting Adaptor Molecular (RIAM) mediates integrin activation by linking RAP1 GTPase to talin, an integrin activator. RIAM’s function in integrin signaling is tightly regulated. In this commentary, we review recent studies of the molecular mechanisms underlying RIAM autoinhibition via both intramolecular interaction and oligomer assembly, and the phosphorylation-dependent activation of RIAM.


RIAM, Integrin, Phosphorylation, RAP1, FAK, SRC, Lamellipodin

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