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CHL1 promotes Sema3A‐induced growth cone collapse and neurite elaboration through a motif required for recruitment of ERM proteins to the plasma membrane
Author(s) -
Schlatter Monika C.,
Buhusi Mona,
Wright Amanda G.,
Maness Patricia F.
Publication year - 2008
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2007.05013.x
Subject(s) - growth cone , neurite , sema3a , microbiology and biotechnology , biology , ezrin , axon guidance , transmembrane protein , semaphorin , fibronectin , moesin , axon , cytoskeleton , receptor , cell , genetics , extracellular matrix , in vitro
Close homolog of L1 (CHL1) is a transmembrane cell adhesion molecule with unique developmental functions in cortical neuronal positioning and dendritic projection within the L1 family, as well as shared functions in promotion of integrin‐dependent neurite outgrowth and semaphorin3A (Sema3A)‐mediated axon repulsion. The molecular mechanisms by which CHL1 mediates these diverse functions are obscure. Here it is demonstrated using a cytofluorescence assay that CHL1 is able to recruit ezrin, a member of the ezrin‐radixin‐moesin (ERM) family of filamentous actin binding proteins to the plasma membrane, and that this requires a membrane‐proximal motif (RGGKYSV) in the CHL1 cytoplasmic domain. This sequence in CHL1 is shown to have novel functions necessary for Sema3A‐induced growth cone collapse and CHL1‐dependent neurite outgrowth and branching in cortical embryonic neurons. In addition, stimulation of haptotactic cell migration and cellular adhesion to fibronectin by CHL1 depends on the CHL1/ERM recruitment motif. These findings suggest that a direct or indirect interaction between CHL1 and ERM proteins mediates Sema3A‐induced growth cone collapse as well as neurite outgrowth and branching, which are essential determinants of axon guidance and connectivity in cortical development.