A role for p130Cas in mechanotransduction
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Focal adhesions are sites of contact between cells and the extracellular matrix. Sawada et al. (2006) now report that the mechanical stretching of cells forces p130Cas, an adaptor protein at focal adhesions, to undergo a conformational change. This change promotes phosphorylation of p130Cas by Src family kinases and the transduction of integrin-mediated signaling.
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17% of the 93 differentially phosphorylated proteins are known to be central molecular players in focal adhesion signaling.
“17% are known to be central molecular players in focal adhesion sig naling (Fig. 6 D and Fig. S5, A and B; Farhadi and Park, 2025; Fujita et al., 2016; Geiger, 2006; Henderson et al., 2019; Huveneers and Danen, 2009; Islam et al., 2025; Ma”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Geiger, 2006
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Research works printed but not linked: 6
- [1]1. Bershadsky, A. ∙ Kozlov, M. ∙ Geiger, B. Curr. Opin. Cell Biol. 2006; 18:472-481 Crossref Scopus (318) PubMed Google Scholar
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Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis
Walsh, A. E., Davis, B. A., Samuels, J. D., Mills, W. A., Thanos, J. M., Johnson, A. M., Moore, K. A., Puchalski, M. A., Steacy, E. J., Wendell, B. W., et al. (2026) · Journal of Experimental Medicine · doi:10.1084/jem.20260104
- Authors
- Geiger, B.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Geiger, Benjamin
- ORCID
- Geiger, Benjamin
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 127
- Issue
- 5
- Pages
- 879-881
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2074277907
- Cited by
- 43
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2020: 3 · 2017: 4 · 2015: 1 · 2014: 4 · 2012: 1
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2420 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5u54gm064346-10)
- National Institute of General Medical Sciences (U54 GM 64346)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- p130Cas, mechanotransduction, focal adhesions, integrin signaling, Src family kinases, protein phosphorylation, conformational change, extracellular matrix
- MeSH terms
- Biomechanical Phenomena, Humans, Substrate Specificity, Phosphotyrosine, src-Family Kinases, Focal Adhesions, Mechanotransduction, Cellular, Crk-Associated Substrate Protein
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