ERMs colocalize transiently with L1 during neocortical axon outgrowth
- 29 July 2003
- journal article
- research article
- Published by Wiley in Journal of Comparative Neurology
- Vol. 464 (4) , 438-448
Abstract
L1 is a member of the Ig superfamily of cell adhesion molecules (CAMs) that functions in many aspects of neuronal development including axonal outgrowth and neuronal migration. These functions require coordination between L1 and the actin cytoskeleton. Because CAMs and the cytoskeleton do not bind directly, membrane–cytoskeletal linkers (MCLs) such as ankyrin are thought to be crucial to their interactions, but data from a knockout mouse suggest that ankyrin is not necessary for the earliest events attributed to L1 function. Recent findings in hippocampal cell culture show that members of the ERM family of proteins (ezrin, radixin, and moesin) can also serve as MCLs between L1 and actin in neurons. Here, we demonstrate that ERM proteins are expressed in extending neuronal processes in the intermediate zone of the developing cortex, a region that is densely packed with migrating neurons and growing axons. ERMs and L1 are codistributed extensively over a transient time course that coincides with rapid axon growth and cortical expansion. This codistribution is strong at embryonic day 17 and 19 but diminishes by postnatal day 0, at which time ankyrin‐L1 codistribution increases dramatically. These findings suggest that in the developing neocortex, ERMs are the predominant MCL for L1 during migration and axon extension, neither of which requires ankyrin function. Furthermore, these data suggest that there is a developmentally regulated switch in MCL function in the developing brain. J. Comp. Neurol. 464:438–448, 2003.Keywords
This publication has 32 references indexed in Scilit:
- Normal Development of Mice and Unimpaired Cell Adhesion/Cell Motility/Actin-based Cytoskeleton without Compensatory Up-regulation of Ezrin or Radixin in Moesin Gene KnockoutJournal of Biological Chemistry, 1999
- Nervous System Defects of AnkyrinB (−/−) Mice Suggest Functional Overlap between the Cell Adhesion Molecule L1 and 440-kD AnkyrinB in Premyelinated AxonsJournal of Cell Biology, 1998
- The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membraneTrends in Biochemical Sciences, 1998
- Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail AssociationJournal of Cell Biology, 1998
- Ezrin Is an Effector of Hepatocyte Growth Factor–mediated Migration and Morphogenesis in Epithelial CellsJournal of Cell Biology, 1997
- The L1 Family of Neural Cell Adhesion Molecules: Old Proteins Performing New TricksNeuron, 1996
- A new 440-kD isoform is the major ankyrin in neonatal rat brain.Journal of Cell Biology, 1991
- Association of ezrin isoforms with the neuronal cytoskeletonJournal of Neuroscience Research, 1991
- Immunohistological localization of the neural adhesion molecules L1 and N-CAM in the developing hippocampus of the mouseJournal of Neurocytology, 1990
- The role of cytoskeleton in organizing growth cones: a microfilament-associated growth cone component depends upon microtubules for its localization.Journal of Cell Biology, 1989