【摘 要】
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Kindlin-2 belongs to a subfamily of FERM domain containing proteins,which plays key roles in activating integrin transmembrane receptors and mediating cell adhe
【机 构】
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National Laboratory of Biophysics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100
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Kindlin-2 belongs to a subfamily of FERM domain containing proteins,which plays key roles in activating integrin transmembrane receptors and mediating cell adhesion.Compared to conventional FERM domains,kindlin-2 FERM contains an inserted pleckstrin homology (PH) domain that specifically binds to phosphatidylinositol (3,4,5) trisphosphate (PIP3) and regulates the kindlin-2 function.We have determined the crystal structure of kindlin-2 PH domain at 1.9 A resolution,which reveals a conserved PH domain fold with a highly charged and open binding pocket for PIP3 head group.Structural comparison with a previously reported solution structure of kindlin-2 PH domain bound to PIP3 head group reveals that upon PIP3 insertion,there is a significant conformational change of both the highly positively charged loop at the entry of the PIP3 binding pocket and the entire β barrel of the PH domain.We propose that such “induced-fit” type change is crucial for the tight binding of PIP3 to anchor kindlin-2 onto the membrane surface,thereby promoting its binding to integrins.Our results provide important structural insight into kindlin-2-mediated membrane anchoring and integrin activation.
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