Interaction between telencephalin and ERM family proteins mediates dendritic filopodia formation.
Dendritic filopodia are long, thin, actin-rich, and dynamic protrusions that are thought to play a critical role as a precursor of spines during neural development. We reported previously that a telencephalon-specific cell adhesion molecule, telencephalin (TLCN) [intercellular adhesion molecule-5 (ICAM-5)], is highly expressed in dendritic filopodia, facilitates the filopodia formation, and slows spine maturation. Here we demonstrate that TLCN cytoplasmic region binds ERM (ezrin/radixin/moesin) family proteins that link membrane proteins to actin cytoskeleton. In cultured hippocampal neurons, phosphorylated active forms of ERM proteins are colocalized with TLCN in dendritic filopodia, whereas alpha-actinin, another binding partner of TLCN, is colocalized with TLCN at surface membranes of soma and dendritic shafts. Expression of constitutively active ezrin induces dendritic filopodia formation, whereas small interference RNA-mediated knockdown of ERM proteins decreases filopodia density and accelerates spine maturation. These results indicate the important role of TLCN-ERM interaction in the formation of dendritic filopodia, which leads to subsequent synaptogenesis and establishment of functional neural circuitry in the developing brain.
Furutani
Yutaka
Y
Laboratory for Neurobiology of Synapse, RIKEN Brain Science Institute, Saitama, Japan.
Matsuno
Hitomi
H
Kawasaki
Miwa
M
Sasaki
Takehiko
T
Mori
Kensaku
K
Yoshihara
Yoshihiro
Y
D000199:Actins / Q000378:metabolism; D000818:Animals; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D003712:Dendrites / Q000648:ultrastructure*; D003952:Diagnostic Imaging / Q000379:methods; D004622:Embryo, Mammalian; D006624:Hippocampus / Q000166:cytology; D047468:Immunoprecipitation / Q000379:methods; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008954:Models, Biological; D009154:Mutation / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D009474:Neurons / Q000166:cytology*; D011485:Protein Binding; D011554:Pseudopodia / Q000502:physiology*; D020349:Surface Plasmon Resonance / Q000379:methods; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014162:Transfection / Q000379:methods; D020798:Two-Hybrid System Techniques; D000099149:Ezrin
D000199:Actins; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D014157:Transcription Factors; D000099149:Ezrin; C513242:Etv5 protein, mouse; C504585:Icam5 protein, mouse
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