Journal
JOURNAL OF CELL BIOLOGY
Volume 157, Issue 7, Pages 1105-1112Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200111076
Keywords
cell adhesion molecules; neuronal polarity; hippocampus; ezrin; moesin
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Funding
- NCRR NIH HHS [S10 RR0 9145] Funding Source: Medline
- NIAAA NIH HHS [R21 AA012971-01, R21 AA012971, R01 AA014898, R21 AA012971-02, AA12971, R21 AA012971-03] Funding Source: Medline
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A yeast two-hybrid library was screened using the cytoplasmic domain of the axonal cell adhesion molecule L1 to identify binding partners that may be involved in the regulation of L1 function. The intracellular domain of L1 bound to ezrin, a member of the ezrin, radixin, and moesin (ERM) family of membrane-cytoskeleton linking proteins, at a site overlapping that for AP2, a clathrin adaptor. Binding of bacterial fusion proteins confirmed this interaction. To determine whether ERM proteins interact with L1 in vivo, extracellular antibodies to L1 were used to force cluster the protein on cultured hippocampal neurons and PC12 cells, which were then immunolabeled for ERM proteins. Confocal analysis revealed a precise pattern of codistribution between ERMs and L1 clusters in axons and PC12 neurites, whereas ERMs in dendrites and spectrin labeling remained evenly distributed. Transfection of hippocampal neurons grown on an L1 substrate with a dominant negative ERM construct resulted in extensive and abnormal elaboration of membrane protrusions and an increase in axon branching, highlighting the importance of the ERM-actin interaction in axon development. Together, our data indicate that L1 binds directly to members of the ERM family and suggest this association may coordinate aspects or axonal morphogenesis.
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