Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction
Abstract Integrin clusters facilitate mechanical force transmission (mechanotransduction) and regulate biochemical signaling during cell adhesion. However, most studies have focused on rigid substrates. On fluid substrates like supported lipid bilayers (SLBs), integrin ligands are mobile, and adhesi...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-56343-6 |
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| author | Oleg Mikhajlov Ram M. Adar Maria Tătulea-Codrean Anne-Sophie Macé John Manzi Fanny Tabarin Aude Battistella Fahima di Federico Jean-François Joanny Guy Tran van Nhieu Patricia Bassereau |
| author_facet | Oleg Mikhajlov Ram M. Adar Maria Tătulea-Codrean Anne-Sophie Macé John Manzi Fanny Tabarin Aude Battistella Fahima di Federico Jean-François Joanny Guy Tran van Nhieu Patricia Bassereau |
| author_sort | Oleg Mikhajlov |
| collection | DOAJ |
| description | Abstract Integrin clusters facilitate mechanical force transmission (mechanotransduction) and regulate biochemical signaling during cell adhesion. However, most studies have focused on rigid substrates. On fluid substrates like supported lipid bilayers (SLBs), integrin ligands are mobile, and adhesive complexes are traditionally thought unable to anchor for cell spreading. Here, we demonstrate that cells spread on SLBs coated with Invasin, a high-affinity integrin ligand. Unlike SLBs functionalized with RGD peptides, integrin clusters on Invasin-SLBs grow in size and complexity comparable to those on glass. While actomyosin contraction dominates adhesion maturation on stiff substrates, we find that on fluid SLBs, integrin mechanotransduction and cell spreading rely on dynein pulling forces along microtubules perpendicular to the membranes and microtubules pushing on adhesive complexes, respectively. These forces, potentially present on non-deformable surfaces, are revealed in fluid substrate systems. Supported by a theoretical model, our findings demonstrate a mechanical role for microtubules in integrin clustering. |
| format | Article |
| id | doaj-art-af5a36801f974fdf8853d39bd1b93ef9 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-af5a36801f974fdf8853d39bd1b93ef92025-02-02T12:33:09ZengNature PortfolioNature Communications2041-17232025-01-0116111710.1038/s41467-025-56343-6Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransductionOleg Mikhajlov0Ram M. Adar1Maria Tătulea-Codrean2Anne-Sophie Macé3John Manzi4Fanny Tabarin5Aude Battistella6Fahima di Federico7Jean-François Joanny8Guy Tran van Nhieu9Patricia Bassereau10Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSLInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieInstitute for Integrative Biology of the Cell (I2BC), CNRS UMR9198, Inserm U1280, 1 Avenue de la TerrasseInstitut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie CurieAbstract Integrin clusters facilitate mechanical force transmission (mechanotransduction) and regulate biochemical signaling during cell adhesion. However, most studies have focused on rigid substrates. On fluid substrates like supported lipid bilayers (SLBs), integrin ligands are mobile, and adhesive complexes are traditionally thought unable to anchor for cell spreading. Here, we demonstrate that cells spread on SLBs coated with Invasin, a high-affinity integrin ligand. Unlike SLBs functionalized with RGD peptides, integrin clusters on Invasin-SLBs grow in size and complexity comparable to those on glass. While actomyosin contraction dominates adhesion maturation on stiff substrates, we find that on fluid SLBs, integrin mechanotransduction and cell spreading rely on dynein pulling forces along microtubules perpendicular to the membranes and microtubules pushing on adhesive complexes, respectively. These forces, potentially present on non-deformable surfaces, are revealed in fluid substrate systems. Supported by a theoretical model, our findings demonstrate a mechanical role for microtubules in integrin clustering.https://doi.org/10.1038/s41467-025-56343-6 |
| spellingShingle | Oleg Mikhajlov Ram M. Adar Maria Tătulea-Codrean Anne-Sophie Macé John Manzi Fanny Tabarin Aude Battistella Fahima di Federico Jean-François Joanny Guy Tran van Nhieu Patricia Bassereau Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction Nature Communications |
| title | Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction |
| title_full | Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction |
| title_fullStr | Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction |
| title_full_unstemmed | Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction |
| title_short | Cell adhesion and spreading on fluid membranes through microtubules-dependent mechanotransduction |
| title_sort | cell adhesion and spreading on fluid membranes through microtubules dependent mechanotransduction |
| url | https://doi.org/10.1038/s41467-025-56343-6 |
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