Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force

Clémence Vigouroux; Véronique Henriot; Christophe Le Clainche

doi:10.1038/s41467-020-16922-1

Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force

Nat Commun. 2020 Jun 19;11(1):3116. doi: 10.1038/s41467-020-16922-1.

Authors

Clémence Vigouroux¹, Véronique Henriot¹, Christophe Le Clainche²

Affiliations

¹ Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France.
² Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France. christophe.leclainche@i2bc.paris-saclay.fr.

Abstract

Cells reinforce adhesion strength and cytoskeleton anchoring in response to the actomyosin force. The mechanical stretching of talin, which exposes cryptic vinculin-binding sites, triggers this process. The binding of RIAM to talin could regulate this mechanism. However, the mechanosensitivity of the talin-RIAM complex has never been tested. It is also not known whether RIAM controls the mechanosensitivity of the talin-vinculin complex. To address these issues, we designed an in vitro microscopy assay with purified proteins in which the actomyosin force controls RIAM and vinculin-binding to talin. We demonstrate that actomyosin triggers RIAM dissociation from several talin domains. Actomyosin also provokes the sequential exchange of RIAM for vinculin on talin. The effect of RIAM on this force-dependent binding of vinculin to talin varies from one talin domain to another. This mechanism could allow talin to biochemically code a wide range of forces by selecting different combinations of partners.

Publication types

Research Support, Non-U.S. Gov't
Video-Audio Media

MeSH terms

Actomyosin / isolation & purification
Actomyosin / metabolism*
Adaptor Proteins, Signal Transducing / genetics
Adaptor Proteins, Signal Transducing / isolation & purification
Adaptor Proteins, Signal Transducing / metabolism*
Animals
Genes, Reporter / genetics
Luminescent Proteins / genetics
Membrane Proteins / genetics
Membrane Proteins / isolation & purification
Membrane Proteins / metabolism*
Microscopy, Fluorescence
Molecular Imaging
Muscle, Skeletal
Rabbits
Recombinant Proteins / genetics
Recombinant Proteins / isolation & purification
Recombinant Proteins / metabolism
Talin / genetics
Talin / isolation & purification
Talin / metabolism*
Vinculin / genetics
Vinculin / isolation & purification
Vinculin / metabolism*

Substances

APBB1IP protein, human
Adaptor Proteins, Signal Transducing
Luminescent Proteins
Membrane Proteins
Recombinant Proteins
TLN1 protein, human
Talin
VCL protein, human
Vinculin
Actomyosin