Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge
The extracellular matrix protein Reelin, secreted by Cajal-Retzius (CR) cells in the marginal zone (MZ) of the cerebral cortex, is important for neuronal migration during development. Two lipoprotein receptors for Reelin have been identified, apolipoprotein E receptor 2 (ApoER2) and the very low den...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2009-07-01
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| Series: | Communicative & Integrative Biology |
| Online Access: | https://www.tandfonline.com/doi/10.4161/cib.2.4.8614 |
| _version_ | 1797683940338696192 |
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| author | Xuejun Chai Eckart Förster Shanting Zhao Hans H. Bock Michael Frotscher |
| author_facet | Xuejun Chai Eckart Förster Shanting Zhao Hans H. Bock Michael Frotscher |
| author_sort | Xuejun Chai |
| collection | DOAJ |
| description | The extracellular matrix protein Reelin, secreted by Cajal-Retzius (CR) cells in the marginal zone (MZ) of the cerebral cortex, is important for neuronal migration during development. Two lipoprotein receptors for Reelin have been identified, apolipoprotein E receptor 2 (ApoER2) and the very low density lipoprotein receptor (VLDLR). The binding of Reelin to these receptors induces tyrosine phosphorylation of an adapter protein, disabled 1 (Dab1) by src family kinases (SFKs). In the Reelin-deficient mutant reeler, cortical lamination is inverted with many neurons invading the marginal zone and others that are unable to migrate to their destinations and accumulate underneath their predecessors, suggesting a role for Reelin signaling in dynamic cytoskeletal reorganization. At present these effects of Reelin are poorly understood. In our recent study, we showed that Reelin induces serine3 phosphorylation of n-cofilin, an actin-depolymerizing protein promoting the disassembly of F-actin. Phosphorylation of cofilin renders it unable to depolymerize F-actin, thus stabilizing the cytoskeleton. We provided evidence for ApoER2, Dab1, SFKs, and phosphatidylinositol-3-kinase (PI3K) to be involved in Reelin-induced cofilin phosphorylation. We found that phosphorylation of cofilin occurs in the leading processes of radially migrating neurons as they grow towards the Reelin-containing marginal zone. By cofilin phophorylation, Reelin may act as a stop signal for radially migrating neurons. |
| first_indexed | 2024-03-12T00:22:10Z |
| format | Article |
| id | doaj.art-720969f1f58d49349c2683b0d508dd28 |
| institution | Directory Open Access Journal |
| issn | 1942-0889 |
| language | English |
| last_indexed | 2024-03-12T00:22:10Z |
| publishDate | 2009-07-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Communicative & Integrative Biology |
| spelling | doaj.art-720969f1f58d49349c2683b0d508dd282023-09-15T13:02:39ZengTaylor & Francis GroupCommunicative & Integrative Biology1942-08892009-07-012437537710.4161/cib.2.4.8614Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edgeXuejun Chai0Eckart Förster1Shanting Zhao2Hans H. Bock3Michael Frotscher4Albert Ludwig University Freiburg; Freiburg, GermanyAlbert Ludwig University Freiburg; Freiburg, GermanyAlbert Ludwig University Freiburg; Freiburg, GermanyAlbert Ludwig University Freiburg; Freiburg, GermanyAlbert Ludwig University Freiburg; Freiburg, GermanyThe extracellular matrix protein Reelin, secreted by Cajal-Retzius (CR) cells in the marginal zone (MZ) of the cerebral cortex, is important for neuronal migration during development. Two lipoprotein receptors for Reelin have been identified, apolipoprotein E receptor 2 (ApoER2) and the very low density lipoprotein receptor (VLDLR). The binding of Reelin to these receptors induces tyrosine phosphorylation of an adapter protein, disabled 1 (Dab1) by src family kinases (SFKs). In the Reelin-deficient mutant reeler, cortical lamination is inverted with many neurons invading the marginal zone and others that are unable to migrate to their destinations and accumulate underneath their predecessors, suggesting a role for Reelin signaling in dynamic cytoskeletal reorganization. At present these effects of Reelin are poorly understood. In our recent study, we showed that Reelin induces serine3 phosphorylation of n-cofilin, an actin-depolymerizing protein promoting the disassembly of F-actin. Phosphorylation of cofilin renders it unable to depolymerize F-actin, thus stabilizing the cytoskeleton. We provided evidence for ApoER2, Dab1, SFKs, and phosphatidylinositol-3-kinase (PI3K) to be involved in Reelin-induced cofilin phosphorylation. We found that phosphorylation of cofilin occurs in the leading processes of radially migrating neurons as they grow towards the Reelin-containing marginal zone. By cofilin phophorylation, Reelin may act as a stop signal for radially migrating neurons.https://www.tandfonline.com/doi/10.4161/cib.2.4.8614 |
| spellingShingle | Xuejun Chai Eckart Förster Shanting Zhao Hans H. Bock Michael Frotscher Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge Communicative & Integrative Biology |
| title | Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge |
| title_full | Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge |
| title_fullStr | Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge |
| title_full_unstemmed | Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge |
| title_short | Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge |
| title_sort | reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n cofilin at the leading edge |
| url | https://www.tandfonline.com/doi/10.4161/cib.2.4.8614 |
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