Intrinsically disordered region of talin’s FERM domain functions as an initial PIP2 recognition site
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 phosphat...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
4 April 2023
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| In: |
Biophysical journal
Year: 2023, Volume: 122, Issue: 7, Pages: 1277-1286 |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2023.02.020 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.bpj.2023.02.020 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0006349523001261 
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| Author Notes: | Jannik Buhr, Florian Franz, and Frauke Gräter |
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| 520 | |a 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-long loop strongly interacts with PIP2 and can facilitate further membrane contacts, including the canonical PIP2 interactions, by serving as a flexible membrane anchor. Under force as present at FAs, the extensible FERM loop ensures talin maintains membrane contacts when pulled away from the membrane by up to 7 nm. We identify key basic residues of the anchor mediating the highly dynamic talin-membrane interaction. Our results put forward an intrinsically disordered loop as a key and highly adaptable PIP2 recognition site of talin and potentially other PIP2-binding mechano-proteins. | ||
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