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CCM1–ICAP-1 complex controls β1 integrin–dependent endothelial contractility and fibronectin remodeling
Open accessAbstract
The endothelial CCM complex regulates blood vessel stability and permeability. Loss-of-function mutations in CCM genes are responsible for human cerebral cavernous malformations (CCMs), which are characterized by clusters of hemorrhagic dilated capillaries composed of endothelium lacking mural cells and altered sub-endothelial extracellular matrix (ECM). Association of the CCM1/2 complex with ICAP-1, an inhibitor of β1 integrin, prompted us to investigate whether the CCM complex interferes with integrin signaling. We demonstrate that CCM1/2 loss resulted in ICAP-1 destabilization, which increased β1 integrin activation and led to increased RhoA-dependent contractility. The resulting abnormal distribution of forces led to aberrant ECM remodeling around lesions of CCM1- and CCM2-deficient mice. ICAP-1–deficient vessels displayed similar defects. We demonstrate that a positive feedback loop between the aberrant ECM and internal cellular tension led to decreased endothelial barrier function. Our data support that up-regulation of β1 integrin activation participates in the progression of CCM lesions by destabilizing intercellular junctions through increased cell contractility and aberrant ECM remodeling.
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“A recent report demonstrated that activation of β1-integrin due to loss of its inhibitor, ICAP-1, in human cerebral cavernous malformations, results in β1-integrin deposition in fibrillar adhesions, increased actin stress fibres and reduced endothelial barrier function35, suggesting that increased β1-integrin activity destabilizes intercellular junctions via increased cell contractility and”
From Endothelial destabilization by angiopoietin-2 via integrin β1 activation (2015) · cites this paper as [35]
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Nobiletti, N., Liu, J., & Glading, A. (2022) · FEBS Journal · doi:10.1111/febs.16627 · Cited by 4
Molecular Genetics of Vascular Malformations
Queisser, A., Boon, L. M., & Vikkula, M. (2018) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0021459.pub2 · Cited by 3
Mládek, A., Skalický, P., Beneš, V., & Bradáč, O. (2020) · Springer eBooks · doi:10.1007/978-3-030-49406-3_3 · Cited by 2
Vascular permeability regulation by fluid shear stress
Kang, N., & Yun, S. (2026) · Mechanobiology · doi:10.1177/29780241261432416 · Cited by 2
Deep-Learning Uncovers certain CCM Isoforms as Transcription Factors.
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Machine Learning Uncovers CCM Isoforms as Transcription FactorsPreprint
Zhang, J., Croft, J., Gao, L., & Sheng, V. S. (2023) · Research Square · doi:10.21203/rs.3.rs-3133629/v1 · Cited by 2
Cerebral Cavernous Malformation (CCM)-like Vessel Lesion in the Aged ANKS1A-deficient Brain
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ICAP‐1 loss impairs CD8+ thymocyte development and leads to reduced marginal zone B cells in mice
Sevilla‐Movilla, S., Fuentes, P., Rodríguez‐García, Y., Arellano‐Sánchez, N., Krenn, P. W., de Val, S. I., Montero‐Herradón, S., García‐Ceca, J., Burdiel-Herencia, V., Gardeta, S. R., et al. (2022) · European Journal of Immunology · doi:10.1002/eji.202149560 · Cited by 1
Self-citationThe CCM complex puts a cap on integrin activity
Short, B. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.2023if
Fu, P., & Natarajan, V. (2015) · Springer eBooks · doi:10.1007/978-3-319-18392-3_5
Cerebral Cavernous Malformations, Molecular Biology, and Genetics
Boulday, G., & Tournier‐Lasserve, E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-812532-8.00011-2
Self-citationHakanpää, L. (2020) · Työväentutkimus Vuosikirja
Faurobert, E., Rome, C., Lisowska, J., Manet, S., Boulday, G., Malbouyres, M., Balland, M., Bouin, A., Kéramidas, M., Bouvard, D., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.2109oia28
Self-citationTension cellulaire et trafic des intégrines
Bouin, A., Kyumurkov, A., Planus, E., & Albigès‐Rizo, C. (2023) · médecine/sciences · doi:10.1051/medsci/2023089
Self-citationCircumferential actomyosin bundles drive endothelial cell deformations to constrict blood vesselsPreprint
Chen, Y., Taberner, N., da Silva, J. A., Kondrychyn, I., Aswani, N., Chen, G., Okada, Y., Lagendijk, A. K., Okuda, S., & Phng, L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.22.630001
Common and distinct circulating microRNAs in four neurovascular disorders
Koskimäki, J., Jhaveri, A., Srinath, A., Bindal, A., Cruz, D. V., Yeradoddi, G. P., Lightle, R., Lee, J. C., Stadnik, A., Iqbal, J., et al. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102189
Metadata
- Authors
- Faurobert, E., Rome, C., Lisowska, J., Manet-Dupé, S., Boulday, G., Malbouyres, M., Balland, M., Bouin, A.-P., Kéramidas, M., Bouvard, D., Coll, J.-L., Ruggiero, F., Tournier-Lasserve, E., & Albiges-Rizo, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- INSERM U823, Institut Albert Bonniot, Grenoble F-38042, France 1
- École Normale Supérieure de Lyon (FR)
- INSERM, UMR-S 740, Université Paris Diderot, Paris F-75010, France 4
- Corresponding author
- Faurobert, Eva
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2013-08-05
- Volume
- 202
- Issue
- 3
- Pages
- 545-561
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3734079
- OpenAlex
- W2117038928
- Cited by
- 114
- References
- 83
- Citations by year
- 2026: 9 · 2025: 3 · 2024: 12 · 2023: 8 · 2022: 9 · 2021: 6 · 2020: 15 · 2019: 4 · 2018: 8 · 2017: 5 · 2016: 7 · 2015: 10 · 2014: 15 · 2013: 3
- FWCI
- 7.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Ligue Contre le Cancer
- Centre National de la Recherche Scientifique
- Topics
- Health Sciences › Medicine › Clinical Neurology › Vascular Malformations Diagnosis and Treatment
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- CCM1, CCM2, beta1 integrin, endothelial contractility, RhoA signaling, extracellular matrix remodeling, fibronectin, cerebral cavernous malformations, endothelial barrier function, intercellular junctions, vascular stability
- MeSH terms
- KRIT1 Protein, Animals, Cell Adhesion, Cells, Cultured, Fibronectins, Humans, Mice, Inbred Strains, Microtubule-Associated Proteins, Models, Biological, Proto-Oncogene Proteins, Mice, Knockout, Integrin beta1, Intracellular Signaling Peptides and Proteins, Mice, Human Umbilical Vein Endothelial Cells
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