Blood: 14-3-3-c-Src-integrator-beta-3 complex is essential for platelet activation!
Last Update: 2020-07-13
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Several adapter molecules bind to the intracellular end of beta-integrator to promote bidirectional signalconducting, which is essential in
formation and hemorrhage
Interfering with integrator-adapter interactions spatially or in time to suppress thrombosis without affecting hemostatic is an attractive strategy for developing safe antithrombotic agents
this study is the first to report the formation of a 14-3-3-c-src-integrin (integrator)-beta-3 complex during platelet activation
14-3-3-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 14-3-3
EL17 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 bleeding
this 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
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