The DOI matches its Crossref record; 48 of the 49 references it cites were found in a registry or an index.
Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
Open accessAbstract
Integrin-mediated cell-ECM (extracellular matrix) adhesion is a fundamental process that controls cell behaviour. For correct cell-ECM adhesion, both the ligand-binding affinity and the spatial organization of integrins must be precisely controlled; how integrins are regulated, however, is not completely understood. Kindlins constitute a family of evolutionarily conserved cytoplasmic components of cell-ECM adhesions that bind to beta-integrin cytoplasmic tails directly and cooperate with talin in integrin activation. In addition, kindlins interact with many components of cell-ECM adhesions--such as migfilin and integrin-linked kinase--to promote cytoskeletal reorganization. Loss of kindlins causes severe defects in integrin signalling, cell-ECM adhesion and cytoskeletal organization, resulting in early embryonic lethality (kindlin-2), postnatal lethality (kindlin-3) and Kindler syndrome (kindlin-1). It is therefore clear that kindlins, together with several other integrin-proximal proteins, are essential for integrin signalling and cell-ECM adhesion regulation.
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“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of β1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004, Larjava et al., 2008, Rognoni et al., 2014).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Larjava et al., 2008
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“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of β1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004, Larjava et al., 2008, Rognoni et al., 2014).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Larjava et al., 2008
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Cites
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
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
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
Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins
Kim, M., Carman, C. V., & Springer, T. A. (2003) · Science · doi:10.1126/science.1084174 · Cited by 786
Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., & Ginsberg, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28071 · Cited by 720
Kindlin-3 is essential for integrin activation and platelet aggregation
Moser, M., Nieswandt, B., Ussar, S., Požgajová, M., & Fässler, R. (2008) · Nature Medicine · doi:10.1038/nm1722 · Cited by 700
Krüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., & Mann, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.033 · Cited by 680
Structural Basis of Integrin Activation by Talin
Wegener, K. L., Partridge, A. W., Han, J., Pickford, A. R., Liddington, R., Ginsberg, M. H., & Campbell, I. D. (2007) · Cell · doi:10.1016/j.cell.2006.10.048 · Cited by 677
Pearson, M. A., Reczek, D., Bretscher, A. P., & Karplus, P. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80836-3 · Cited by 614
Hughes, P. E., Díaz‐González, F., Leong, L., Wu, C., McDonald, J. A., Shattil, S. J., & Ginsberg, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6571 · Cited by 571
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1 of the 49 references couldn’t be matched to a known paper.
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Barczyk, M., Carracedo, S., & Gullberg, D. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0834-6 · Cited by 1,512
Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma
Ji, A. L., Rubin, A. J., Thrane, K., Jiang, S., Reynolds, D. L., Meyers, R. M., Guo, M. G., George, B. M., Mollbrink, A., Bergenstråhle, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.039 · Cited by 1,117
“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of b1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004; Larjava et al., 2008; Rognoni et al., 2014).”
BackgroundPhysical influences of the extracellular environment on cell migration
Charras, G., & Sahai, E. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3897 · Cited by 678
Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
Svensson, L. M., Howarth, K. M., McDowall, A., Patzak, I. M., Evans, R., Ussar, S., Moser, M., Metìn, A., Fried, M., Tomlinson, I. P. M., et al. (2009) · Nature Medicine · doi:10.1038/nm.1931 · Cited by 418
The insider's guide to leukocyte integrin signalling and function
Hogg, N., Patzak, I. M., & Willenbrock, F. W. (2011) · Nature reviews. Immunology · doi:10.1038/nri2986 · Cited by 402
Metadata
- Authors
- Larjava, H., Plow, E. F., & Wu, C.
- Affiliations
- University of British Columbia (CA)
- Cleveland Clinic (US)
- University of Pittsburgh (US)
- Venue
- The EMBO Reports
- Published
- 2008-11-07
- Volume
- 9
- Issue
- 12
- Pages
- 1203-1208
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2603460
- OpenAlex
- W2159437476
- Cited by
- 268
- References
- 49
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 7 · 2023: 7 · 2022: 14 · 2021: 16 · 2020: 12 · 2019: 13 · 2018: 11 · 2017: 15 · 2016: 10 · 2015: 12 · 2014: 21 · 2013: 21 · 2012: 16
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (P01HL073311)
- National Institute of General Medical Sciences (GM 65188, R01GM065188)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK54639, R01DK054639)
- National Institute of Dental and Craniofacial Research (R01DE016099, DE016099)
- 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 › Cell Biology › Skin and Cellular Biology Research
- Keywords
- kindlin, integrin signaling, cell-matrix adhesion, talin, integrin activation, integrin-linked kinase, cytoskeletal organization, Kindler syndrome, kindlin-1, Kindlin-2, kindlin-3, embryonic lethality
- MeSH terms
- Animals, Carrier Proteins, Cell Adhesion, Disease, Humans, Signal Transduction, Integrins, Cell-Matrix Junctions
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