The role of kindlins in cell biology and relevance to human disease
Abstract
The kindlins represent a class of focal adhesion proteins implicated in integrin activation. They comprise three evolutionarily conserved members, kindlin-1, kindlin-2 and kindlin-3, that share considerable sequence and structural similarities. The kindlins have a bipartite FERM (four point one protein, ezrin, radixin, moesin) domain interrupted by a pleckstrin homology domain and can bind directly to various classes of integrins as well as participate in inside-out integrin activation. They are encoded by three different genes, namely KIND1 (FERMT1; chromosome 20p12.3), KIND2 (FERMT2; chromosome 14q22.1) and KIND3 (FERMT3; chromosome 11q13.1). Loss-of-function mutations in KIND1 and KIND3 cause Kindler syndrome and leukocyte adhesion deficiency-III syndrome, respectively, although no human disease has yet been associated with KIND2 gene pathology. In this review, we focus on the cellular functions of the kindlins and their clinical relevance.
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Kindlin-2 is a focal adhesion protein involved in integrin activation and can directly bind F-actin to modulate its organisation.
“Kindlin-2 is a focal adhesion (FA) protein involved in integrin activation [77] and is also able to directly bind filamentous actin (F-actin) to modulate its organisation [12].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [77]
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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 · see citing works
Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
Larjava, H., Plow, E. F., & Wu, C. (2008) · The EMBO Reports · doi:10.1038/embor.2008.202 · Cited by 268 · see citing works
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Dourlen, P., Kilinc, D., Malmanche, N., Chapuis, J., & Lambert, J.-C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02004-0 · Cited by 168 · see citing works
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- Authors
- Lai-Cheong, J. E., Parsons, M., & McGrath, J. A.
- Affiliations
- King's College London (GB)
- Corresponding author
- McGrath, J.A.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 42
- Issue
- 5
- Pages
- 595-603
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W2002340857
- Cited by
- 92
- References
- 2
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 1 · 2022: 6 · 2021: 5 · 2020: 5 · 2019: 5 · 2018: 7 · 2017: 8 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 7 · 2012: 4
- FWCI
- 0.65
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- Wellcome Trust
- National Institute for Health and Care Research
- 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, kindlin-1, Kindlin-2, kindlin-3, FERM domain, pleckstrin homology domain, integrin activation, inside-out signaling, focal adhesions, Kindler syndrome, loss-of-function mutations, human disease
- MeSH terms
- Animals, Carrier Proteins, Cytoskeletal Proteins, Humans, Membrane Proteins, Muscle Proteins, Neoplasm Proteins, Neoplasms, Syndrome, Integrins, Protein Isoforms, Focal Adhesions, Genetic Diseases, Inborn
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