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Functional binding interaction identified between the axonal CAM L1 members of the ERM family


Dickson, TC and Mintz, CD and Benson, DL and Salton, SRJ, Functional binding interaction identified between the axonal CAM L1 members of the ERM family, Journal of Cell Biology, 157, (7) pp. 1105-1112. ISSN 0021-9525 (2002) [Refereed Article]

DOI: doi:10.1083/jcb.200111076


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 of axonal morphogenesis.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Biochemistry and cell biology
Research Field:Cellular interactions (incl. adhesion, matrix, cell wall)
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Dickson, TC (Professor Tracey Dickson)
ID Code:32822
Year Published:2002
Web of Science® Times Cited:120
Deposited By:Pathology
Deposited On:2005-08-01
Last Modified:2006-05-05

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