西亚试剂：A novel membrane-dependent on/off switch mechanism of talin

发布时间：2025-10-05

A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion

Xianqiang Song， Jun Yang， Jamila Hirbawi， Sheng Ye， H Dhanuja Perera， Esen Goksoy， Pallavi Dwivedi， Edward F Plow， Rongguang Zhang， Jun Qin

The activation of heterodimeric (α/β) integrin transmembrane receptors by cytosolic protein talin is crucial for regulating diverse cell-adhesion-dependent processes， including blood coagulation， tissue remodeling， and cancer metastasis. This process is triggered by the coincident binding of N-terminal FERM (four-point-one-protein/ezrin/radixin/moesin) domain of talin (talin-FERM) to the inner membrane surface and integrin β cytoplasmic tail， but how these binding events are spatiotemporally regulated remains obscure. Here we report the crystal structure of a dormant talin， revealing how a C-terminal talin rod segment (talin-RS) self-masks a key integrin-binding site on talin-FERM via a large interface. Unexpectedly， the structure also reveals a distinct negatively charged surface on talin-RS that electrostatically hinders the talin-FERM binding to the membrane. Such a dual inhibitory topology for talin is consistent with the biochemical and functional data， but differs significantly from a previous model. We show that upon enrichment with phosphotidylinositol-4，5-bisphosphate (PIP2) – a known talin activator， membrane strongly attracts a positively charged surface on talin-FERM and simultaneously repels the negatively charged surface on talin-RS. Such an electrostatic “pull-push” process promotes the relief of the dual inhibition of talin-FERM， which differs from the classic “steric clash” model for conventional PIP2-induced FERM domain activation. These data therefore unravel a new type of membrane-dependent FERM domain regulation and illustrate how it mediates the talin on/off switches to regulate integrin transmembrane signaling and cell adhesion.

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