Cited by 170Neurogenesis and neuroplasticity mechanismsCell Adhesion Molecules ResearchMultiple Sclerosis Research Studies

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Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

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Chun, Soo Jin, Rasband, Matthew N., Sidman, Richard L., Habib, Amyn A., Vartanian, Timothy·2003·The Journal of Cell Biology

DOI 10.1083/jcb.200304154PMC PMC2173507

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Abstract

Early steps in myelination in the central nervous system (CNS) include a specialized and extreme form of cell spreading in which oligodendrocytes extend large lamellae that spiral around axons to form myelin. Recent studies have demonstrated that laminin-2 (LN-2; α2β1γ1) stimulates oligodendrocytes to extend elaborate membrane sheets in vitro (cell spreading), mediated by integrin α6β1. Although a congenital LN-2 deficiency in humans is associated with CNS white matter changes, LN-2–deficient (dy/dy) mice have shown abnormalities primarily within the peripheral nervous system. Here, we demonstrate a critical role for LN-2 in CNS myelination by showing that dy/dy mice have quantitative and morphologic defects in CNS myelin. We have defined the molecular pathway through which LN-2 signals oligodendrocyte cell spreading by demonstrating requirements for phosphoinositide 3-kinase activity and integrin-linked kinase (ILK). Interaction of oligodendrocytes with LN-2 stimulates ILK activity. A dominant negative ILK inhibits LN-2–induced myelinlike membrane formation. A critical component of the myelination signaling cascade includes LN-2 and integrin signals through ILK.

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Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
Delcommenne, M., Tan, C., Gray, V., Rue, L., Woodgett, J. R., & Dedhar, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11211 · Cited by 1,102
Paxillin and focal adhesion signalling
Turner, C. E. (2000) · Nature Cell Biology · doi:10.1038/35046659 · Cited by 839
Integrin-linked kinase (ILK) and its interactors
Wu, C., & Dedhar, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200108077 · Cited by 449
Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells
Persad, S., Attwell, S., Gray, V., Delcommenne, M., Troussard, A. A., Sanghera, J. S., & Dedhar, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3207 · Cited by 428
Myelinated nerve fibres in the CNS
Hildebrand, C., Remahl, S., Persson, H., & Bjartmar, C. (1993) · Progress in Neurobiology · doi:10.1016/0301-0082(93)90015-k · Cited by 395
Initial events of myelination involve Fyn tyrosine kinase signalling
Umemori, H., Satot, S., Yagi, T., Aizawal, S., & Yamamoto, T. S. (1994) · Nature · doi:10.1038/367572a0 · Cited by 387
Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulationPreprint
Sakai, T., Li, S., Docheva, D., Grashoff, C., Sakai, K., Kostka, G., Braun, A., Pfeifer, A., Yurchenco, P. D., & Fässler, R. (2003) · Genes & Development · doi:10.1101/gad.255603 · Cited by 378
Requirement for Activation of the Serine-Threonine Kinase Akt (Protein Kinase B) in Insulin Stimulation of Protein Synthesis but Not of Glucose Transport
Kitamura, T., Ogawa, W., Sakaue, H., Hino, Y., Kuroda, S., Takata, M., Matsumoto, M., Maeda, T., Konishi, H., Kikkawa, U., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3708 · Cited by 328
Dependence of nodal sodium channel clustering on paranodal axoglial contact in the developing CNS
Rasband, M. N., Peles, E., Trimmer, J. S., Levinson, S. R., Lux, S. E., & Shrager, P. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-17-07516.1999 · Cited by 325
Self-citation
Conditional disruption of β1 integrin in Schwann cells impedes interactions with axons
Feltri, M. L., Porta, D. G., Previtali, S. C., Nodari, A., Migliavacca, B., Cassetti, A., Littlewood-Evans, A., Reichardt, L. F., Messing, A., Quattrini, A., et al. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109021 · Cited by 325

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Neural plasticity and addiction: integrin‐linked kinase and cocaine behavioral sensitization
Chen, Q., Xiong, X., Lee, T. H., Liu, Y., Wetsel, W. C., & Zhang, X. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05619.x · Cited by 31
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The molecular regulation of oligodendrocyte development and CNS myelination by ECM proteins
Yamada, M., Iwase, M., Sasaki, B., & Suzuki, N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.952135 · Cited by 24
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Tohda, C., Nakanishi, R., & Kadowaki, M. (2006) · Neurosignals · doi:10.1159/000108936 · Cited by 24
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Multiple roles for integrins in Drosophila glial development
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Schultz, K. (2012) · doi:10.53846/goediss-1535
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Chua, S. J. (2011) · TSpace (University of Toronto)
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References
(2006) · Elsevier eBooks · doi:10.1016/b978-0-443-07271-0.50022-7
Integrin Signaling
Wu, X., & Guan, J. (2008) · Wiley eBooks · doi:10.1002/9780470048672.wecb253
Molecular mechanisms of myelin membrane biogenesis
Trajković, K. (2008) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3427
Pinch2 is a novel regulator of myelination in the Central Nervous SystemPreprint
de Faria, J. P., Vale-Silva, R. S., Fässler, R., Werner, H. B., & Relvas, J. B. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.04.483000
Focal adhesion kinase, a major regulator of oligodendrocyte morphological maturation and myelination
Lafrenaye, A. D. (2010) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/9rxs-er88
Role of γ1 Laminin and Its KDI Peptide in the Central Nervous System
Wikstén, M. (2007) · Työväentutkimus Vuosikirja
Analyse histologique et fonctionnelle du développement de précurseurs neuraux dérivés de cellules souches pluripotentes induites humaines greffés dans le cortex de la souris
Raïs, C. (2019) · theses.fr (ABES) · doi:10.70675/e853aef3za211z4be9z822fzfb9846d925a7
Rôle de la protéine de densité post-synaptique 95 (PSD-95) dans la myélinisation du système nerveux central
Masson, M. L. P. (2024) · theses.fr (ABES) · doi:10.70675/7f680c8dz2453z40c7z9047z982a66a8bfd5
GPR17 + Oligodendrocyte Lineage Cells Regulate the Critical Period of Brain Development Through Novel Chondroitin Sulfate‐Rich Structures
Tanaka, T., Kerever, A., Suzuki, Y., Kunitomi, T., Kato, K., Yamashita, Y., Higashi, K., Akazawa, C., Saitow, F., Suzuki, H., et al. (2026) · Glia · doi:10.1002/glia.70188
Integrin-Linked Kinase Suppression Reduces SPARC's Effect on Intraocular Pressure and Extracellular Matrix
Guo, C. W., Birrell, S., Baillargeon, S., Koster, K. G., Jeppesen, B., Zheng, Y., Castillejos, A. G., Murali, A., Kang, M. H., Scott-McKean, J. J., et al. (2026) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.67.10.53
Laminin Expression and Function in the Central Nervous System
Xu, L., Yuan, S., & Yao, Y. (2026) · Proteoglycan Research · doi:10.1002/pgr2.70058
Biology of Demyelinating Diseases
Pham-Dinh, D., & Baumann, N. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_16
The role of beta1 integrin in myelination and remyelination
Lee, K. K. C. (2009) · uO Research (University of Ottawa) · doi:10.20381/ruor-19952
Identification and Characterization of the Expression Profile of Oligodendrocyte-Derived and Associated Proteins via Unilateral X-Irradation of the Rat Optic Nerve
Greco, N. J. (2005) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/dv1h-4389
Niemann-Pick Type C Disease: Molecular Mechanisms of Neurodegeneration and Targets for Therapeutic Intervention.
Yu, T. (2013) · Deep Blue (University of Michigan)

Authors: Chun, S. J., Rasband, M. N., Sidman, R. L., Habib, A. A., & Vartanian, T.
Affiliations: Beth Israel Deaconess Medical Center (US)
UConn Health (US)
Corresponding author: Vartanian, Timothy
ORCID: Rasband, Matthew N.
Sidman, Richard L.
Habib, Amyn A.
Vartanian, Timothy
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2003-10-27
Volume: 163
Issue: 2
Pages: 397-408
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200304154
PMC: PMC2173507
OpenAlex: W2120316837
Cited by: 170
References: 41
Citations by year: 2026: 4 · 2025: 3 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 5 · 2019: 10 · 2018: 4 · 2017: 8 · 2016: 6 · 2015: 10 · 2014: 4 · 2013: 7 · 2012: 8
FWCI: 2.44
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Funders: National Institutes of Health (5k02ns002028-04)
National Institute of Neurological Disorders and Stroke (K02 NS02028, P01 NS 38475, R01NS044916, P01NS038475, R01NS042317, R01 NS42317)
Topics: Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Health Sciences › Medicine › Clinical Neurology › Multiple Sclerosis Research Studies
Keywords: integrin-linked kinase, laminin-2, CNS myelination, alpha6beta1 integrin, phosphatidylinositol 3-kinase, myelination, integrin signaling
MeSH terms: Scaffold Protein ILK, Adenoviridae, Animals, Axons, Cell Survival, Cells, Cultured, Central Nervous System, Cytoskeletal Proteins, Enzyme Activation, Homozygote, Laminin, Mice, Mutant Strains, Mutation, Myelin Sheath, Oligodendroglia, Optic Nerve, Phosphoproteins, Cell Adhesion Molecules, Rats, Sprague-Dawley, Protein Serine-Threonine Kinases, Phosphatidylinositol 3-Kinases, Mice, Rats, Paxillin

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Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

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