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  Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin

Kelley, C. F., Litschel, T., Schumacher, S., Dedden, D., Schwille, P., & Mizuno, N. (2020). Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin. eLife, 9: e56110. doi:10.7554/eLife.56110.

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 Creators:
Kelley, Charlotte F.1, Author              
Litschel, Thomas2, Author              
Schumacher, Stephanie3, Author              
Dedden, Dirk1, Author              
Schwille, Petra2, Author              
Mizuno, Naoko1, Author              
Affiliations:
1Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1688137              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: PI(4,5)P2; actin; autoinhibition; cell biology; focal adhesion; molecular biophysics; none; structural biology; talin; vinculin.
 Abstract: Focal adhesions (FA) are large macromolecular assemblies which help transmit mechanical forces and regulatory signals between the extracellular matrix and an interacting cell. Two key proteins talin and vinculin connecting integrin to actomyosin networks in the cell. Both proteins bind to F-actin and each other, providing a foundation for network formation within FAs. However, the underlying mechanisms regulating their engagement remain unclear. Here, we report on the results of in vitro reconstitution of talin-vinculin-actin assemblies using synthetic membrane systems. We find that neither talin nor vinculin alone recruit actin filaments to the membrane. In contrast, phosphoinositide-rich membranes recruit and activate talin, and the membrane-bound talin then activates vinculin. Together, the two proteins then link actin to the membrane. Encapsulation of these components within vesicles reorganized actin into higher-order networks. Notably, these observations were made in the absence of applied force, whereby we infer that the initial assembly stage of FAs is force independent. Our findings demonstrate that the local membrane composition plays a key role in controlling the stepwise recruitment, activation, and engagement of proteins within FAs.

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Language(s): eng - English
 Dates: 2020-07-13
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.56110
PMID: 32657269
PMC: PMC7384861
 Degree: -

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Project name : FocAd/H2020 European Research Council
Grant ID : -
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)
Project name : Horizon 2020 Framework Programme/Marie Sklodowska-Curie Action (C.F.K.)
Grant ID : -
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)
Project name : European Molecular Biology Organization/EMBO Long-term Fellowship Award (C.F.K.); Alexander von Humboldt-Stiftung/Research Fellowship for Postdoctoral Researchers (C.F.K.); Boehringer Ingelheim Stiftung (Plus 3) N.M.; European Molecular Biology Organization (Young Investigator Award) N.M.
Grant ID : -
Funding program : -
Funding organization : diverse

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 9 Sequence Number: e56110 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X