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The Rap1-RIAM pathway prefers ?2 integrins #MMPMID26679542
Calderwood DA
Blood 2015[Dec]; 126 (25): 2658-9 PMID26679542show ga
In vitro studies strongly implicate the talin-binding Ras-related protein 1 (Rap1) effector, Rap1-guanosine triphosphate?interacting adapter molecule (RIAM), in integrin activation.1 Yet, the RIAM knockout mouse is viable and fertile and exhibits no platelet adhesion or aggregation defects,2 casting doubt on the in vivo role of RIAM. In this issue of Blood, Su et al3 and Klapproth et al4 now show that RIAM is required for ?2 integrin?dependent leukocyte adhesion and trafficking in vitro and in vivo, but apparently not for all Rap- and talin-meditated activation of ?1 and ?3 integrins.