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Stress fiber strain recognition by the LIM protein testin is cryptic and mediated by RhoA

View ORCID ProfileStefano Sala, View ORCID ProfilePatrick W. Oakes
doi: https://doi.org/10.1101/2021.01.21.427693
Stefano Sala
Department of Cell and Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153, USA
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  • ORCID record for Stefano Sala
Patrick W. Oakes
Department of Cell and Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153, USA
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  • For correspondence: poakes@luc.edu
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Abstract

The actin cytoskeleton is a key regulator of mechanical processes in cells. The family of LIM domain proteins have recently emerged as important mechanoresponsive cytoskeletal elements capable of sensing strain in the actin cytoskeleton. The mechanisms regulating this mechanosensitive behavior, however, remain poorly understood. Here we show that the LIM domain protein testin is peculiar in that despite the full-length protein primarily appearing diffuse in the cytoplasm, the C-terminal LIM domains alone recognize focal adhesions and strained actin while the N-terminal domains alone recognize stress fibers. Phosphorylation mutations in the dimerization regions of testin, however, reveal its mechanosensitivity and cause it to relocate to focal adhesions and sites of strain in the actin cytoskeleton. Finally, we demonstrate activated RhoA causes testin to adorn stress fibers and become mechanosensitive. Together, our data show that testin’s mechanoresponse is regulated in cells and provide new insights into LIM domain protein recognition of the actin cytoskeleton mechanical state.

Competing Interest Statement

The authors have declared no competing interest.

  • Abbreviations

    CA
    constitutively active
    CR
    cysteine rich
    DN
    dominant-negative
    FA
    focal adhesion
    FHL
    four- and-a-half LIM
    FL
    full-length
    HFF
    human foreskin fibroblast
    LDP
    LIM domain protein
    LIM
    Lin-11, Isl-1, Mec-3
    MEF
    mouse embryonic fibroblast
    PET
    Prickle, Espinas, Testin
    SF
    stress fiber
    SFSS
    stress fiber strain site
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    Posted March 31, 2021.
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    Stress fiber strain recognition by the LIM protein testin is cryptic and mediated by RhoA
    Stefano Sala, Patrick W. Oakes
    bioRxiv 2021.01.21.427693; doi: https://doi.org/10.1101/2021.01.21.427693
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    Stress fiber strain recognition by the LIM protein testin is cryptic and mediated by RhoA
    Stefano Sala, Patrick W. Oakes
    bioRxiv 2021.01.21.427693; doi: https://doi.org/10.1101/2021.01.21.427693

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