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Calsyntenins function as synaptogenic adhesion molecules in concert with neurexins

Authors
 Ji Won Um  ;  Gopal Pramanik  ;  Ji Seung Ko  ;  Min-Young Song  ;  Dongmin Lee  ;  Hyun Kim  ;  Kang-Sik Park  ;  Thomas C. Südhof  ;  Katsuhiko Tabuchi  ;  Jaewon Ko 
Citation
 CELL REPORTS, Vol.6(6) : 1096-1109, 2014 
Journal Title
 CELL REPORTS 
Issue Date
2014
MeSH
Animals ; Calcium-Binding Proteins/metabolism* ; Cell Adhesion Molecules, Neuronal/metabolism* ; Cell Differentiation/physiology ; Female ; HEK293 Cells ; Hippocampus/cytology ; Hippocampus/metabolism ; Humans ; Membrane Proteins/metabolism* ; Mice ; Mice, Inbred ICR ; Nerve Tissue Proteins/metabolism* ; Neurons/cytology* ; Neurons/metabolism ; Pregnancy ; Synapses/metabolism ; Synaptic Transmission
Abstract
Multiple synaptic adhesion molecules govern synapse formation. Here, we propose calsyntenin-3/alcadein-β as a synapse organizer that specifically induces presynaptic differentiation in heterologous synapse-formation assays. Calsyntenin-3 (CST-3) is highly expressed during various postnatal periods of mouse brain development. The simultaneous knockdown of all three CSTs, but not CST-3 alone, decreases inhibitory, but not excitatory, synapse densities in cultured hippocampal neurons. Moreover, the knockdown of CSTs specifically reduces inhibitory synaptic transmission in vitro and in vivo. Remarkably, the loss of CSTs induces a concomitant decrease in neuron soma size in a non-cell-autonomous manner. Furthermore, α-neurexins (α-Nrxs) are components of a CST-3 complex involved in CST-3-mediated presynaptic differentiation. However, CST-3 does not directly bind to Nrxs. Viewed together, these data suggest that the three CSTs redundantly regulate inhibitory synapse formation, inhibitory synapse function, and neuron development in concert with Nrxs.
Files in This Item:
T201400700.pdf Download
DOI
10.1016/j.celrep.2014.02.010
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers
Yonsei Authors
Um, Ji Won(엄지원)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/138201
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