4.7 Article

Detection of surface forces by the cell-wall mechanosensor Wsc1 in yeast

Journal

DEVELOPMENTAL CELL
Volume 56, Issue 20, Pages 2856-+

Publisher

CELL PRESS
DOI: 10.1016/j.devcel.2021.09.024

Keywords

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Funding

  1. MEIC, Spain [BFU2017-84508-P]
  2. Regional Government of Castile and Leon [SA073U14]
  3. Centre National de la Recherche Scientifique (CNRS)
  4. Agence Nationale pour la Recherche [ANR-14-CE11-0009-02, ANR-20-CE130003-01]
  5. La Ligue Contre le Cancer [EL2021.LNCC/NiM]
  6. European Research Council (ERC CoG Forcaster'') [647073]
  7. Agence Nationale de la Recherche (ANR) [ANR-14-CE11-0009] Funding Source: Agence Nationale de la Recherche (ANR)

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The study on the conserved CW sensor Wsc1 in fission yeast revealed the formation of micrometer-sized clusters at sites of force application onto the CW, which assembled within minutes of CW compression and disassembled upon relaxation. Wsc1 accumulates to sites of enhanced mechanical stress through reduced lateral diffusivity, mediated by the binding of its extracellular WSC domain to CW polysaccharides, independently of canonical polarity, trafficking, and downstream CW regulatory pathways. Wsc1 may represent an autonomous module to detect and transduce local surface forces onto the CW.
Surface receptors of animal cells, such as integrins, promote mechanosensation by forming clusters as signaling hubs that transduce tensile forces. Walled cells of plants and fungi also feature surface sensors, with long extracellular domains that are embedded in their cell walls (CWs) and are thought to detect injuries and promote repair. How these sensors probe surface forces remains unknown. By studying the conserved CW sensor Wsc1 in fission yeast, we uncovered the formation of micrometer-sized clusters at sites of force application onto the CW. Clusters assembled within minutes of CW compression, in dose dependence with mechanical stress and disassembled upon relaxation. Our data support that Wsc1 accumulates to sites of enhanced mechanical stress through reduced lateral diffusivity, mediated by the binding of its extracellular WSC domain to CW polysaccharides, independent of canonical polarity, trafficking, and downstream CW regulatory pathways. Wsc1 may represent an autonomous module to detect and transduce local surface forces onto the CW.

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