Blood: 14-3-3-c-Src-integrator-beta-3 complex is essential for platelet activation!

Several adapter molecules bind to the intracellular end of beta-integrator to promote bidirectional signalconducting, which is essential inthrombosisformation and hemorrhageInterfering with integrator-adapter interactions spatially or in time to suppress thrombosis without affecting hemostatic is an attractive strategy for developing safe antithrombotic agentsthis study is the first to report the formation of a 14-3-3-c-src-integrin (integrator)-beta-3 complex during platelet activation14-3-3-c-Src interaction is mediated by sH2 domain on upper protein fragments (PE16) and c-Src on 14-3-3," while 14-3-3-src-integrators The interaction of -beta 3 is mediated by the keatstf fragment (KF7) on the eskvfylkmyryl fragment (EL17) on 14-3-3EL17 die inhibitors or FK7 peptides can interfere with the formation of 14-3-3-c-c-Src-src-beta-3 complex, selectively inhibit the transmission of extracellular-intracellular signals of beta 3, and do not affect the interaction of the integrator-fiunophin, thereby inhibiting thrombosis without causing visible bleedingthis study characterizes the previously unknown 14-3-3-c-Src-src-src-beta-3 complex in platelets and provides a new strategy for the development of safe and effective antithrombotic therapy