Intrinsically disordered region of talin's FERM domain functions as an initial PIP₂ recognition site.

ABSTRACT: Focal adhesions (FAs) mediate the interaction of the cytoskeleton with the extracellular matrix in a highly dynamic fashion. Talin is a central regulator, adaptor protein, and mechano-sensor of FA complexes. For recruitment and firm attachment at FAs, talin's N-terminal FERM domain binds to phosphatidylinositol 4,5-bisphosphate (PIP₂)-enriched membranes. A newly published autoinhibitory structure of talin-1, where the known PIP₂ interaction sites are covered up, lead us to hypothesize that a hitherto less examined loop insertion of the FERM domain acts as an additional and initial site of contact. We evaluated direct interactions of talin-1 with a PIP₂ membrane by means of atomistic molecular dynamics simulations. We show that this unstructured, 33-residue-

SUBMITTER: Buhr J 

PROVIDER: S-EPMC10111347 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature