Y. K. Takada

FGF9, a potent mitogen, is a new ligand for integrin αvβ3, and the FGF9 mutant defective in integrin binding acts as an antagonist.

This study identifies FGF9 as a new ligand for integrin αvβ3 and shows that a mutant defective in integrin binding acts as an antagonist by suppressing FGF9 signaling.

The heparin-binding domain of VEGF165 directly binds to integrin αvβ3 and plays a critical role in signaling.

This study identifies the heparin-binding domain of VEGF165 as critical for integrin αvβ3 binding and signaling, showing its role in mitogenic activity.

Pro-inflammatory chemokines CCL5, CXCL12, and CX3CL1 bind to and activate platelet integrin αIIbβ3 in an allosteric manner.

This study identifies CCL5, CXCL12, and CX3CL1 as novel ligands for platelet integrin αIIbβ3 that allosterically activate it, linking inflammation to thrombosis.

Anti-PF4 (heparin-independent)/PF4 complex induces allosteric activation of integrins αIIbβ3 and αvβ3, a potential mechanism of vaccine-induced thrombotic thrombocytopenia (VITT) and autoimmune diseases

This paper shows that the PF4/anti-PF4 complex activates integrins αIIbβ3 and αvβ3 through site 2 binding, suggesting a mechanism for VITT and autoimmune diseases.

The C-type lectin domain of CD62P (P-selectin) is an integrin ligand.

This study identifies the C-type lectin domain of CD62P as a potential integrin ligand through docking simulations and experimental validation, showing distinct binding sites from glycan recognition.