Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation

@inproceedings{Zhu2017StructureOR,
  title={Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation},
  author={Liang Zhu and Jun Yang and Thomas Bromberger and Ashley Holly and Fan Lu and Huan Liu and Kevin Haoyu Sun and Sarah Klapproth and Jamila Hirbawi and Tatiana V. Byzova and Edward F Plow and Markus Moser and Jun Qin},
  booktitle={Nature Communications},
  year={2017}
}
Activation of transmembrane receptor integrin by talin is essential for inducing cell adhesion. However, the pathway that recruits talin to the membrane, which critically controls talin’s action, remains elusive. Membrane-anchored mammalian small GTPase Rap1 is known to bind talin-F0 domain but the binding was shown to be weak and thus hardly studied. Here we show structurally that talin-F0 binds to human Rap1b like canonical Rap1 effectors despite little sequence homology, and disruption of… CONTINUE READING
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