Membrane-induced 2D phase separation of the focal adhesion protein talin

Thomas Litschel (), Charlotte F. Kelley, Xiaohang Cheng, Leon Babl, Naoko Mizuno, Lindsay B. Case and Petra Schwille ()
Additional contact information
Thomas Litschel: Max Planck Institute of Biochemistry
Charlotte F. Kelley: Max Planck Institute of Biochemistry
Xiaohang Cheng: Massachusetts Institute of Technology
Leon Babl: Max Planck Institute of Biochemistry
Naoko Mizuno: Max Planck Institute of Biochemistry
Lindsay B. Case: Massachusetts Institute of Technology
Petra Schwille: Max Planck Institute of Biochemistry

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Focal adhesions form liquid-like assemblies around activated integrin receptors at the plasma membrane. How they achieve their flexible properties is not well understood. Here, we use recombinant focal adhesion proteins to reconstitute the core structural machinery in vitro. We observe liquid-liquid phase separation of the core focal adhesion proteins talin and vinculin for a spectrum of conditions and interaction partners. Intriguingly, we show that binding to PI(4,5)P2-containing membranes triggers phase separation of these proteins on the membrane surface, which in turn induces the enrichment of integrin in the clusters. We suggest a mechanism by which 2-dimensional biomolecular condensates assemble on membranes from soluble proteins in the cytoplasm: lipid-binding triggers protein activation and thus, liquid-liquid phase separation of these membrane-bound proteins. This could explain how early focal adhesions maintain a structured and force-resistant organization into the cytoplasm, while still being highly dynamic and able to quickly assemble and disassemble.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-49222-z Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49222-z

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-49222-z

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().