Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge.
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Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge. / Chai, Xuejun; Förster, Eckart; Zhao, Shanting; Bock, Hans H; Frotscher, Michael.
In: Commun Integr Biol, Vol. 2, No. 4, 4, 2009, p. 375-377.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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T1 - Reelin acts as a stop signal for radially migrating neurons by inducing phosphorylation of n-cofilin at the leading edge.
AU - Chai, Xuejun
AU - Förster, Eckart
AU - Zhao, Shanting
AU - Bock, Hans H
AU - Frotscher, Michael
PY - 2009
Y1 - 2009
N2 - 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 phosphorylation, Reelin may act as a stop signal for radially migrating neurons.
AB - 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 phosphorylation, Reelin may act as a stop signal for radially migrating neurons.
U2 - 10.4161/cib.2.4.8614
DO - 10.4161/cib.2.4.8614
M3 - SCORING: Zeitschriftenaufsatz
VL - 2
SP - 375
EP - 377
IS - 4
M1 - 4
ER -