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Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails
Abstract
Cells recognize and respond to their extracellular environment through transmembrane receptors such as integrins, which physically connect the extracellular matrix to the cytoskeleton. Integrins provide the basis for the assembly of intracellular signaling platforms that link to the cytoskeleton and influence nearly every aspect of cell physiology; however, integrins possess no enzymatic or actin-binding activity of their own and thus rely on adaptor molecules, which bind to the short cytoplasmic tails of integrins, to mediate and regulate these functions. Many adaptors compete for relatively few binding sites on integrin tails, so regulatory mechanisms have evolved to reversibly control the spatial and temporal binding of specific adaptors. This Commentary discusses the adaptor proteins that bind directly to the tails of β integrins and, using talin, tensin, filamin, 14-3-3 and integrin-linked kinase (ILK) as examples, describes the ways in which their binding is regulated.
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“These tails also act as a hub to form and regulate intracellular protein complexes [292–294].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [293]
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Cites
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
Getting to the site of inflammation: the leukocyte adhesion cascade updated
Ley, K., Laudanna, C., Cybulsky, M. I., & Nourshargh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2156 · Cited by 4,354
Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
Geiger, B., Bershadsky, A. D., Pankov, R. G., & Yamada, K. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35099066 · Cited by 2,213
Humphries, J. D., Byron, A., & Humphries, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03098 · Cited by 1,711
Integrin-regulated FAK–Src signaling in normal and cancer cells
Mitra, S. K., & Schlaepfer, D. D. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.08.011 · Cited by 1,641
Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation
Tadokoro, S., Shattil, S. J., Eto, K., Tai, V., Liddington, R., de Pereda, J. M., Ginsberg, M. H., & Calderwood, D. (2003) · Science · doi:10.1126/science.1086652 · Cited by 1,211
Functional atlas of the integrin adhesome
Zaidel‐Bar, R., Itzkovitz, S., Ma’ayan, A., Iyengar, R., & Geiger, B. (2007) · Nature Cell Biology · doi:10.1038/ncb0807-858 · Cited by 1,182
Hannigan, G. E., Leung-Hagesteijn, C., Fitz-Gibbon, L., Coppolino, M. G., Radeva, G., Filmus, J., Bell, J. C., & Dedhar, S. (1996) · Nature · doi:10.1038/379091a0 · Cited by 1,116
Ramirez, A., Fisher, G., George, E. L., Sanning, E., Forouzani, M., Allen, J., Bak, R., Halley, W., Wheeler, G., her, et al. (2003) · Cited by 960
Vinculin controls focal adhesion formation by direct interactions with talin and actin
Humphries, J. D., Wang, P., Streuli, C. H., Geiger, B., Humphries, M. J., & Ballestrem, C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200703036 · Cited by 910
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Rovensky, Y. A. (2011) · Humana Press eBooks · doi:10.1007/978-1-61779-304-2_4 · Cited by 1
Bourget, J., Morcos, M., Zaniolo, K., Guérin, S. L., & Proulx, S. (2015) · Advances in Biological Chemistry · doi:10.4236/abc.2015.52007 · Cited by 1
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BRONSON, R. A. (2009) · American Journal of Reproductive Immunology · doi:10.1111/j.1600-0897.2009.00758.x · Cited by 1
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Hopkins, P. N. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-1366-4.00008-1 · Cited by 1
Characterization of a germline variant TNS1 c.2999-1G > C in a hereditary cancer syndrome family
Di, X., Wang, D., Wu, J., Zhu, X., Wang, Y., Yan, J., Wen, L., Jiang, H., Wen, D., Shu, B., et al. (2024) · Gene · doi:10.1016/j.gene.2024.148304 · Cited by 1
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Roles of Integrins in the Development and Progression of Squamous Cell Carcinomas
Lamar, J. M., & DiPersio, C. M. (2010) · Springer eBooks · doi:10.1007/978-1-4419-7203-3_2 · Cited by 1
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Jo, M. H., Li, J., Jaumouillé, V., Hao, Y., Coppola, J. D., Yan, J., Waterman, C. M., Springer, T. A., & Ha, T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.08.495291
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li, X. (2014) · University Library - University of Saskatchewan (University of Saskatchewan)
Metadata
- Authors
- Legate, K. R., & Fässler, R.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- Department of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany
- ORCID
- Legate, Kyle R.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2009-01-15
- Volume
- 122
- Issue
- 2
- Pages
- 187-198
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2092447350
- Cited by
- 370
- References
- 175
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 6 · 2023: 11 · 2022: 18 · 2021: 18 · 2020: 18 · 2019: 17 · 2018: 17 · 2017: 19 · 2016: 28 · 2015: 24 · 2014: 28 · 2013: 23 · 2012: 47
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- 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
- beta-integrin, integrin cytoplasmic tail, adaptor proteins, talin, tensin, filamin, 14-3-3 proteins, integrin-linked kinase, integrin signaling, binding regulation, cell adhesion
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cytoplasm, Cytoskeletal Proteins, Humans, Microfilament Proteins, Molecular Sequence Data, Sequence Alignment, Integrin beta Chains
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