ArticleMolecular biology of the cell2006
Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 116 citations in OpenAlex.
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- Piezo2 channel regulates RhoA and actin cytoskeleton to promote cell mechanobiological responses.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Subcellular domain-dependent molecular hierarchy of SFK and FAK in mechanotransduction and cytokine signaling.Scientific reports · 2017Article
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- Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF.Molecular biology of the cell · 2016Article
- Src Family Tyrosine Kinase Signaling Regulates FilGAP through Association with RBM10.PloS one · 2016Article
- Conformational coupling of integrin and Thy-1 regulates Fyn priming and fibroblast mechanotransduction.The Journal of cell biology · 2015Article
- Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix.Nature communications · 2015Article
- A mechanical-biochemical feedback loop regulates remodeling in the actin cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Early events in cell spreading as a model for quantitative analysis of biomechanical events.Biophysical journal · 2014Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell motility on extracellular matrices critically depends on matrix rigidity, which affects cell adhesion and formation of focal contacts. Receptor-like protein tyrosine phosphatase alpha (RPTPalpha) and the alphavbeta3 integrin form a rigidity-responsive complex at the leading edge. Here we show that the rigidity response through increased spreading and growth correlates with leading edge recruitment of Fyn, but not endogenous c-Src. Recruitment of Fyn requires the palmitoylation site near the N-terminus and addition of that site to c-Src enables it to support a rigidity response. In all cases, the rigidity response correlates with the recruitment of the Src family kinase to early adhesions. The stretch-activated substrate of Fyn and c-Src, p130Cas, is also required for a rigidity response and it is phosphorylated at the leading edge in a Fyn-dependent process. A possible mechanism for the fibronectin rigidity response involves force-dependent Fyn phosphorylation of p130Cas with rigidity-dependent displacement. With the greater displacement of Fyn from p130Cas on softer surfaces, there will be less phosphorylation. These studies emphasize the importance of force and nanometer-level movements in cell growth and function.
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