Reelin Binds α3β1 Integrin and Inhibits Neuronal Migration
Open accessAbstract
Mice that are mutant for Reelin or Dab1, or doubly mutant for the VLDL receptor (VLDLR) and ApoE receptor 2 (ApoER2), show disorders of cerebral cortical lamination. How Reelin and its receptors regulate laminar organization of cerebral cortex is unknown. We show that Reelin inhibits migration of cortical neurons and enables detachment of neurons from radial glia. Recombinant and native Reelin associate with alpha3beta1 integrin, which regulates neuron-glia interactions and is required to achieve proper laminar organization. The effect of Reelin on cortical neuronal migration in vitro and in vivo depends on interactions between Reelin and alpha3beta1 integrin. Absence of alpha3beta1 leads to a reduction of Dab1, a signaling protein acting downstream of Reelin. Thus, Reelin may arrest neuronal migration and promote normal cortical lamination by binding alpha3beta1 integrin and modulating integrin-mediated cellular adhesion.
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Reelin binds to VLDLR, apolipoprotein E receptor 2, and α3β1 integrin.
“Reelin binds to several protein receptors, including very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor 2 and α3β1 integrin [144–146].”
From Consensus Paper: Pathological Role of the Cerebellum in Autism (2012) · cites this paper as [146]
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- Authors
- Dulabon, L., Olson, E. C., Taglienti, M. G., Eisenhuth, S., McGrath, B., Walsh, C. A., Kreidberg, J. A., & Anton, E. S.
- Affiliations
- Pennsylvania State University (US)
- Beth Israel Deaconess Medical Center (US)
- Harvard University (US)
- Corresponding author
- Anton, E.S
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 27
- Issue
- 1
- Pages
- 33-44
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2139474686
- Cited by
- 577
- References
- 52
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 14 · 2023: 8 · 2022: 10 · 2021: 13 · 2020: 18 · 2019: 13 · 2018: 11 · 2017: 16 · 2016: 23 · 2015: 17 · 2014: 19 · 2013: 19 · 2012: 16
- FWCI
- 10.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS038097, P01NS039404)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- reelin, alpha3beta1 integrin, neuronal migration, cortical lamination, Dab1, VLDL receptor, ApoER2, radial glia, neuron-glia interactions, integrin-mediated adhesion, cortical development
- MeSH terms
- Reelin Protein, Animals, Antibodies, Monoclonal, Cell Movement, Cells, Cultured, Cerebral Cortex, Humans, Immunohistochemistry, Mice, Neurologic Mutants, Nerve Tissue Proteins, Neurons, Precipitin Tests, Receptors, Cell Surface, Serine Endopeptidases, Cell Adhesion Molecules, Neuronal, Integrins, Extracellular Matrix Proteins, Integrin alpha3beta1, Adaptor Proteins, Signal Transducing, Mice
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