Document Detail


EphB receptors regulate dendritic spine morphogenesis through the recruitment/phosphorylation of focal adhesion kinase and RhoA activation.
MedLine Citation:
PMID:  16298995     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Dendritic filopodia are small protrusions on the surface of neuronal dendrites that transform into dendritic spines upon synaptic contact with axon terminals. The formation of dendritic spines is a critical aspect of synaptic development. Dendritic spine morphogenesis is characterized by filopodia shortening followed by the formation of mature mushroom-shaped spines. Here we show that activation of the EphB receptor tyrosine kinases in cultured hippocampal neurons by their ephrinB ligands induces morphogenesis of dendritic filopodia into dendritic spines. This appears to occur through assembly of an EphB-associated protein complex that includes focal adhesion kinase (FAK), Src, Grb2, and paxillin and the subsequent activations of FAK, Src, paxillin, and RhoA. Furthermore, Cre-mediated knock-out of loxP-flanked fak or RhoA inhibition blocks EphB-mediated morphogenesis of dendritic filopodia. Finally, EphB-mediated RhoA activation is disrupted by FAK knock-down. These data suggest that EphB receptors are upstream regulators of FAK in dendritic filopodia and that FAK-mediated RhoA activation contributes to assembly of actin filaments in dendritic spines.
Authors:
Michael L Moeller; Yang Shi; Louis F Reichardt; Iryna M Ethell
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2005-11-18
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-17     Completed Date:  2006-03-17     Revised Date:  2011-01-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1587-98     Citation Subset:  IM    
Affiliation:
Division of Biomedical Sciences, University of California Riverside, Riverside, California 92521, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Dendritic Spines / ultrastructure*
Embryo, Mammalian
Focal Adhesion Protein-Tyrosine Kinases / metabolism*
Hippocampus / ultrastructure
Ligands
Mice
Neurons / cytology,  ultrastructure
Phosphorylation
Receptors, Eph Family / physiology*
rhoA GTP-Binding Protein / metabolism*
Grant Support
ID/Acronym/Agency:
MH67121/MH/NIMH NIH HHS; NS19090/NS/NINDS NIH HHS; R01 MH067121-04/MH/NIMH NIH HHS
Chemical
Reg. No./Substance:
0/Ligands; EC 2.7.10.1/Receptors, Eph Family; EC 2.7.10.2/Focal Adhesion Protein-Tyrosine Kinases; EC 3.6.5.2/rhoA GTP-Binding Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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