Integrin-mediated signal transduction
Open accessAbstract
Integrins, expressed on virtually every cell type, are proteins that mediated cellular interactions with components of the extracellular matrix (ECM) and cell surface integral plasma membrane proteins. In addition, integrins interact with the cytoskeleton and through this process participate in cell migration, tissue organization, cell growth, haemostasis, inflammation, target recognition of lymphocytes and the differentiation of many cell types. Signals generated from ligand-integrin interactions are propagated via the integrin cytoplasmic tails to signal transduction pathways within the cell (outside-in signalling). Information from within the cell can also be transmitted to the outside via integrin affinity modulation (inside-out signalling). Protein tyrosine phosphorylation has a central role in integrin-initiated cell signalling, leading to cytoskeletal organization and focal adhesion formation. This review will examine the current understanding of integrin function, focusing on the intracellular consequences of integrin-ligand interaction.
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Cells embedded within a tissue interact with the extracellular matrix to develop cell type-dependent features such as morphology, function, proliferation, differentiation, gene expression pattern, and even survival.
“Cells embedded within a tissue interact with the extracellular matrix to develop cell type-dependent features such as morphology, function, proliferation, differentiation, gene expression pattern, and even survival (Dike and Farmer, 1988; Longhurst and Jennings, 1998; Damsky and Ilić, 2002).”
From In Vitro research Reproducibility: Keeping up High Standards (2019) · cites this paper as Longhurst and Jennings, 1998
The Introduction and Conclusion describe integrin-mediated responses to the extracellular matrix as affecting cellular functions in cell type-dependent ways. The paper also links these interactions to cell growth, differentiation, cell shape and regulation of gene expression (Integrin-mediated signal transduction; The role of phosphatidylinositol turnover in integrin-mediated signalling; pages unavailable). The passages found do not establish the claim that these interactions determine cell survival. (LLM, conf=0.84)
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- 2 Marlin S. D. and Springer T. A. (1987) Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-asociated antigen I (LFA-1). Cell 51: 813-819
- 83 Polte T. R. and Hanks S. K. (1995) Interaction between focal adhesion kinase and crk-associated tyrosine kinase substrate p130cas. Proc. Natl. Acad. Sci. USA 92: 10678-10682
- 119 Pelham R. J. and Wang Y. I. (1997) Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. USA 94: 13661-13665
- 136 Chen H.-C. and Guan J.-L. (1994) Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA 91: 10148-10152
- 139 Sjaastad M. D., Angres B., Lewis R. S. and Nelson W. J. (1994) Feedback regulation of cell-substratum adhesion by integrin mediated intracellular Ca 2 signaling. Proc. Natl. Acad. Sci. USA 91: 821-828
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Achache, H., & Revel, A. (2006) · Human Reproduction Update · doi:10.1093/humupd/dml004 · Cited by 952 · see citing works
In Vitro research Reproducibility: Keeping up High Standards
Hirsch, C., & Schildknecht, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01484 · Cited by 161 · see citing works
- Authors
- Longhurst, C. M., & Jennings, L. K.
- Affiliations
- University of Tennessee Health Science Center (US)
- ORCID
- Jennings, L. K.
- Venue
- Cellular and Molecular Life Sciences (CMLS)
- Published
- 1998-06-01
- Volume
- 54
- Issue
- 6
- Pages
- 514-526
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11147418
- OpenAlex
- W2057698056
- Cited by
- 181
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 1 · 2023: 3 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 1 · 2015: 4 · 2014: 2 · 2013: 4 · 2012: 3
- FWCI
- 6.07
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL53514, R01HL053514)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- integrins, signal transduction, extracellular matrix, outside-in signalling, inside-out signalling, tyrosine phosphorylation, cytoskeleton, focal adhesions, cell migration, integrin cytoplasmic tail
- MeSH terms
- Calcium, Cytoskeleton, Enzyme Activation, Membrane Proteins, Phosphatidylinositols, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Signal Transduction, Cell Adhesion Molecules, Integrins, Focal Adhesion Protein-Tyrosine Kinases
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