The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Integrin-mediated mechanotransduction
Open accessAbstract
Cells can detect and react to the biophysical properties of the extracellular environment through integrin-based adhesion sites and adapt to the extracellular milieu in a process called mechanotransduction. At these adhesion sites, integrins connect the extracellular matrix (ECM) with the F-actin cytoskeleton and transduce mechanical forces generated by the actin retrograde flow and myosin II to the ECM through mechanosensitive focal adhesion proteins that are collectively termed the “molecular clutch.” The transmission of forces across integrin-based adhesions establishes a mechanical reciprocity between the viscoelasticity of the ECM and the cellular tension. During mechanotransduction, force allosterically alters the functions of mechanosensitive proteins within adhesions to elicit biochemical signals that regulate both rapid responses in cellular mechanics and long-term changes in gene expression. Integrin-mediated mechanotransduction plays important roles in development and tissue homeostasis, and its dysregulation is often associated with diseases.
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Cites
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Concepts of extracellular matrix remodelling in tumour progression and metastasis
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Integrins as biomechanical sensors of the microenvironment
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Vascular Smooth Muscle Cells and Arterial Stiffening: Relevance in Development, Aging, and Disease
Lacolley, P., Regnault, V., Segers, P., & Laurent, S. (2017) · Physiological Reviews · doi:10.1152/physrev.00003.2017 · Cited by 734
Piezos thrive under pressure: mechanically activated ion channels in health and disease
Murthy, S. E., Dubin, A. E., & Patapoutian, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.92 · Cited by 582
Metadata
- Authors
- Sun, Z., Guo, S. S., & Fässler, R.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2016-11-08
- Volume
- 215
- Issue
- 4
- Pages
- 445-456
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2549070824
- Cited by
- 1,079
- References
- 19
- FWCI
- 46.55
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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