Integrins and Extracellular Matrix in Mechanotransduction
Open accessAbstract
Integrins bind extracellular matrix fibrils and associate with intracellular actin filaments through a variety of cytoskeletal linker proteins to mechanically connect intracellular and extracellular structures. Each component of the linkage from the cytoskeleton through the integrin-mediated adhesions to the extracellular matrix therefore transmits forces that may derive from both intracellular, myosin-generated contractile forces and forces from outside the cell. These forces activate a wide range of signaling pathways and genetic programs to control cell survival, fate, and behavior. Additionally, cells sense the physical properties of their surrounding environment through forces exerted on integrin-mediated adhesions. This article first summarizes current knowledge about regulation of cell function by mechanical forces acting through integrin-mediated adhesions and then discusses models for mechanotransduction and sensing of environmental forces.
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A multitude of ECM components provide cues to induce transdifferentiation through mechanical signalling.
“These findings suggest a multitude of ECM components provide cues to induce transdifferentiation through mechanical signalling73.”
From Cell diversity and plasticity during atrioventricular heart valve EMTs (2023) · cites this paper as [73]
The MATRIX RIGIDITY AND SPREAD AREA section (page unavailable) reports that ECM stiffness affects differentiation and is associated with epithelial–mesenchymal transition in breast cancer cells. SIGNALING PATHWAYS AND GENE EXPRESSION (page unavailable) also describes force-dependent TGFβ activation and fibroblast-to-myofibroblast differentiation. These examples support mechanical cues affecting cell phenotype, but the paper does not establish that a multitude of distinct ECM components induce transdifferentiation. (LLM, conf=0.82)
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“These fi ndings suggest a multitude of ECM components provide cues to induce transdifferentiation through mechanical signalling 73 .”
Background
- Authors
- Schwartz, M. A.
- Affiliations
- University of Virginia (US)
- Corresponding author
- Schwartz, M. A.
- ORCID
- Schwartz, M. A.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-11-17
- Volume
- 2
- Issue
- 12
- Pages
- a005066-a005066
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC2982167
- OpenAlex
- W2116517871
- Cited by
- 662
- References
- 1
- Citations by year
- 2026: 41 · 2025: 39 · 2024: 36 · 2023: 48 · 2022: 30 · 2021: 50 · 2020: 58 · 2019: 40 · 2018: 44 · 2017: 46 · 2016: 32 · 2015: 41 · 2014: 51 · 2013: 35 · 2012: 49
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (R0147214)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Keywords
- integrins, extracellular matrix, mechanotransduction, integrin-mediated adhesion, cytoskeletal linker proteins, F-actin, mechanosensing
- MeSH terms
- Cytoskeleton, Environment, Extracellular Matrix, Gene Expression Regulation, Models, Biological, Signal Transduction, Integrins, Cell-Matrix Junctions, Mechanotransduction, Cellular
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