ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000
Association of beta 1 integrin with focal adhesion kinase and paxillin in differentiating Schwann cells.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 116 citations in OpenAlex.
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- Schwann Cell-Specific Ablation of Beclin 1 Impairs Myelination and Leads to Motor and Sensory Neuropathy in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Family-Wide Photoproximity Profiling of Integrin Protein Social Networks in Cancer.bioRxiv : the preprint server for biology · 2024Article
- Adhesion of retinal cells to gold surfaces by biomimetic molecules.Frontiers in cell and developmental biology · 2024Article
- Cotargeting Phosphoinositide 3-Kinase and Focal Adhesion Kinase Pathways Inhibits Proliferation of NF2 Schwannoma Cells.Molecular cancer therapeutics · 2023Article
- HGF/c-Met/β1-integrin signalling axis induces tunneling nanotubes in A549 lung adenocarcinoma cells.Life science alliance · 2023Article
- Delayed cortical development in mice with a neural specific deletion of β1 integrin.Frontiers in neuroscience · 2023Article
- Involvement of the extracellular matrix and integrin signalling proteins in skeletal muscle glucose uptake.The Journal of physiology · 2022Review
- Actin dynamics in protein homeostasis.Bioscience reports · 2022Review
- Reduced growth rate of aged muscle stem cells is associated with impaired mechanosensitivity.Aging · 2022Article
- Wrestling and Wrapping: A Perspective on SUMO Proteins in Schwann Cells.Biomolecules · 2021Review
- Review
- CBFrontiers in cellular neuroscience · 2020Article
- Atypical Endocannabinoid Signaling Initiates a New Form of Memory-Related Plasticity at a Cortical Input to Hippocampus.Cerebral cortex (New York, N.Y. : 1991) · 2018Article
- Schwann cell durotaxis can be guided by physiologically relevant stiffness gradients.Biomaterials research · 2018Article
- Integrin α2β1 in nonactivated conformation can induce focal adhesion kinase signaling.Scientific reports · 2017Article
- Regulation of Ligand and Shear Stress-induced Insulin-like Growth Factor 1 (IGF1) Signaling by the Integrin Pathway.The Journal of biological chemistry · 2016Article
- Hic-5 mediates the initiation of endothelial sprouting by regulating a key surface metalloproteinase.Journal of cell science · 2016Article
- Regulating Axonal Responses to Injury: The Intersection between Signaling Pathways Involved in Axon Myelination and The Inhibition of Axon Regeneration.Frontiers in molecular neuroscience · 2016Review
- Palladin mediates stiffness-induced fibroblast activation in the tumor microenvironment.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Schwann cells (SCs) differentiate into a myelinating cell when simultaneously adhering to an axon destined for myelination and basal lamina. We are interested in defining the signaling pathway activated by basal lamina. Using SC/sensory neuron (N) cocultures, we identified beta1 integrin and F-actin as components of a pathway leading to myelin gene expression and myelination (Fernandez-Valle et al., 1994, 1997). Here, we show that focal adhesion kinase (FAK) and paxillin are constitutively expressed by SCs contacting axons in the absence of basal lamina. Tyrosine phosphorylation of FAK and paxillin increases as SCs form basal lamina and differentiate. FAK and paxillin specifically coimmunoprecipitate with beta1 integrin in differentiating SC/N cocultures but not SC-only cultures. Paxillin coimmunoprecipitates with FAK and fyn kinase in differentiating SC/N cocultures. A subset of tyrosine-phosphorylated beta1 integrin, FAK, and paxillin molecules reside in the insoluble, F-actin-rich fraction of differentiating cocultures. Cytochalasin D, an actin depolymerizing agent, decreases tyrosine phosphorylation of FAK and paxillin and their association with beta1 integrin and causes a dose-dependent increase in the abundance of insoluble FAK and paxillin complexes. Collectively, our work indicates that beta1 integrin, FAK, paxillin, and fyn kinase form an actin-associated complex in SCs adhering to basal lamina in the presence of axons. This complex may be important for initiating the process of SC differentiation into a myelinating cell.
Indexed as
Identifiers
10804218PMC6772705W1552994237What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.