Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin phosphorylation at serine3
Open accessAbstract
The extracellular matrix protein Reelin, secreted by Cajal-Retzius cells in the marginal zone of the cortex, controls the radial migration of cortical neurons. Reelin signaling involves the lipoprotein receptors apolipoprotein E receptor 2 (ApoER2) and very low density lipoprotein receptor (VLDLR), the adapter protein Disabled1 (Dab1), and phosphatidylinositol-3-kinase (PI3K). Eventually, Reelin signaling acts on the cytoskeleton; however, these effects on cytoskeletal organization have remained elusive. In Reelin-deficient mutant mice, most cortical neurons are unable to migrate to their destinations, suggesting a role for Reelin signaling in the dynamic cytoskeletal reorganization that is required for neurons to migrate. Here, we show that Reelin signaling leads to serine3 phosphorylation of n-cofilin, an actin-depolymerizing protein that promotes the disassembly of F-actin. Phosphorylation at serine3 renders n-cofilin unable to depolymerize F-actin, thereby stabilizing the cytoskeleton. We provide evidence for ApoER2, Dab1, Src family kinases (SFKs), and PI3K to be involved in n-cofilin serine3 phosphorylation. Phosphorylation of n-cofilin takes place in the leading processes of migrating neurons as they approach the Reelin-containing marginal zone. Immunostaining for phospho-cofilin in dissociated reeler neurons is significantly increased after incubation in Reelin-containing medium compared with control medium. In a stripe choice assay, neuronal processes are stable on Reelin-coated stripes but grow on control stripes by forming lamellipodia. These novel findings suggest that Reelin-induced stabilization of neuronal processes anchors them to the marginal zone which appears to be required for the directional migration process.
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Reelin binding to ApoER2 induces binding of Dab1 to its cytoplasmic NPxY motif, resulting in phosphorylation of specific tyrosines, PI3K activation, and n-cofilin phosphorylation in leading processes of migrating neurons.
“Reelin binding to ApoER2 induces binding of the adaptor protein Dab1 to its cytoplasmic NPxY motif [10], [11], resulting in the phosphorylation of specific tyrosines [12], [13], PI3K activation, and n-cofilin phosphorylation in the leading processes of migrating neurons [9], [14].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [14]
The Abstract reports Reelin-induced n-cofilin phosphorylation in the leading processes of migrating neurons. The section ‘Reelin-induced n-cofilin serine3 phosphorylation is mediated by Dab1, SFKs and PI3K’ reports that PI3K inhibition reduces this phosphorylation, but does not establish the separately stated step of PI3K activation. The NPxY-motif and specific-tyrosine clauses have separate citations in the citing sentence and are not assessed against this source. (LLM, conf=0.86)
Experimental — accuracy not yet measuredActivation of apoE receptor family member, LRP8/ApoER2, inhibits the function of n-cofilin and this subsequently leads to stabilization of actin filaments.
“one study demonstrated that activation of apoE receptor family member, LRP8/ApoER2, inhibits the function of n-cofilin and this subsequently leads to stabilization of actin filaments (Chai et al., 2009) (Fig. 2).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Chai et al., 2009
Actin polymerization and dendritic spine growth exhibit a net increase in the presence of Reelin, and mice that overexpress Reelin have higher spine density and increased spine complexity.
“actin polymerization and dendritic spine growth exhibit a net increase in the presence of Reelin, and mice that overexpress Reelin have higher spine density and increased spine complexity [64, 65].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [64]
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BackgroundRole for Reelin in stabilizing cortical architecture
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BackgroundEmerging topics in Reelin function
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- Authors
- Chai, X., Förster, E., Zhao, S., Bock, H. H., & Frotscher, M.
- Affiliations
- University of Freiburg (DE)
- Universität Hamburg (DE)
- Corresponding author
- Frotscher, Michael
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-01-07
- Volume
- 29
- Issue
- 1
- Pages
- 288-299
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6664910
- OpenAlex
- W2117547988
- Cited by
- 202
- References
- 72
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 8 · 2022: 11 · 2021: 10 · 2020: 11 · 2019: 7 · 2018: 10 · 2017: 15 · 2016: 13 · 2015: 8 · 2014: 23 · 2013: 12 · 2012: 16
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (FO 223/6-1, SFB 592)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- reelin, neuronal migration, radial migration, cortical neurons, ApoER2, VLDLR, phosphatidylinositol 3-kinase, Src family kinases, F-actin depolymerization, lamellipodia, reeler mice
- MeSH terms
- Reelin Protein, Actins, Animals, Cell Movement, Cells, Cultured, Cerebral Cortex, Embryo, Mammalian, Enzyme Inhibitors, Humans, Mice, Neurologic Mutants, Mice, Transgenic, Mutation, Nerve Tissue Proteins, Neurons, Phosphorylation, Receptors, Cell Surface, Receptors, LDL, Serine, Serine Endopeptidases, Subcellular Fractions, Transfection, Down-Regulation, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Receptors, Lipoprotein, src-Family Kinases, Phosphatidylinositol 3-Kinases, LDL-Receptor Related Proteins, Cofilin 1, Mice, Lim Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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