Computational model of integrin adhesion elongation under an actin fiber.
Cells create physical connections with the extracellular environment through adhesions. Nascent adhesions form at the leading edge of migrating cells and either undergo cycles of disassembly and reassembly, or elongate and stabilize at the end of actin fibers. How adhesions assemble has been address...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2023-07-01
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| Series: | PLoS Computational Biology |
| Online Access: | https://doi.org/10.1371/journal.pcbi.1011237 |
| _version_ | 1797774500815699968 |
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| author | Samuel Campbell Michelle C Mendoza Aravind Rammohan Matthew E McKenzie Tamara C Bidone |
| author_facet | Samuel Campbell Michelle C Mendoza Aravind Rammohan Matthew E McKenzie Tamara C Bidone |
| author_sort | Samuel Campbell |
| collection | DOAJ |
| description | Cells create physical connections with the extracellular environment through adhesions. Nascent adhesions form at the leading edge of migrating cells and either undergo cycles of disassembly and reassembly, or elongate and stabilize at the end of actin fibers. How adhesions assemble has been addressed in several studies, but the exact role of actin fibers in the elongation and stabilization of nascent adhesions remains largely elusive. To address this question, here we extended our computational model of adhesion assembly by incorporating an actin fiber that locally promotes integrin activation. The model revealed that an actin fiber promotes adhesion stabilization and elongation. Actomyosin contractility from the fiber also promotes adhesion stabilization and elongation, by strengthening integrin-ligand interactions, but only up to a force threshold. Above this force threshold, most integrin-ligand bonds fail, and the adhesion disassembles. In the absence of contraction, actin fibers still support adhesions stabilization. Collectively, our results provide a picture in which myosin activity is dispensable for adhesion stabilization and elongation under an actin fiber, offering a framework for interpreting several previous experimental observations. |
| first_indexed | 2024-03-12T22:22:02Z |
| format | Article |
| id | doaj.art-ac53764c4e7045f5a2372c1d5c8b0811 |
| institution | Directory Open Access Journal |
| issn | 1553-734X 1553-7358 |
| language | English |
| last_indexed | 2024-03-12T22:22:02Z |
| publishDate | 2023-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Computational Biology |
| spelling | doaj.art-ac53764c4e7045f5a2372c1d5c8b08112023-07-23T05:31:05ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582023-07-01197e101123710.1371/journal.pcbi.1011237Computational model of integrin adhesion elongation under an actin fiber.Samuel CampbellMichelle C MendozaAravind RammohanMatthew E McKenzieTamara C BidoneCells create physical connections with the extracellular environment through adhesions. Nascent adhesions form at the leading edge of migrating cells and either undergo cycles of disassembly and reassembly, or elongate and stabilize at the end of actin fibers. How adhesions assemble has been addressed in several studies, but the exact role of actin fibers in the elongation and stabilization of nascent adhesions remains largely elusive. To address this question, here we extended our computational model of adhesion assembly by incorporating an actin fiber that locally promotes integrin activation. The model revealed that an actin fiber promotes adhesion stabilization and elongation. Actomyosin contractility from the fiber also promotes adhesion stabilization and elongation, by strengthening integrin-ligand interactions, but only up to a force threshold. Above this force threshold, most integrin-ligand bonds fail, and the adhesion disassembles. In the absence of contraction, actin fibers still support adhesions stabilization. Collectively, our results provide a picture in which myosin activity is dispensable for adhesion stabilization and elongation under an actin fiber, offering a framework for interpreting several previous experimental observations.https://doi.org/10.1371/journal.pcbi.1011237 |
| spellingShingle | Samuel Campbell Michelle C Mendoza Aravind Rammohan Matthew E McKenzie Tamara C Bidone Computational model of integrin adhesion elongation under an actin fiber. PLoS Computational Biology |
| title | Computational model of integrin adhesion elongation under an actin fiber. |
| title_full | Computational model of integrin adhesion elongation under an actin fiber. |
| title_fullStr | Computational model of integrin adhesion elongation under an actin fiber. |
| title_full_unstemmed | Computational model of integrin adhesion elongation under an actin fiber. |
| title_short | Computational model of integrin adhesion elongation under an actin fiber. |
| title_sort | computational model of integrin adhesion elongation under an actin fiber |
| url | https://doi.org/10.1371/journal.pcbi.1011237 |
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