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PMID:20537373

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Citation

Uemura, T, Lee, SJ, Yasumura, M, Takeuchi, T, Yoshida, T, Ra, M, Taguchi, R, Sakimura, K and Mishina, M (2010) Trans-synaptic interaction of GluRdelta2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum. Cell 141:1068-79

Abstract

Elucidation of molecular mechanisms that regulate synapse formation is required for the understanding of neural wiring, higher brain functions, and mental disorders. Despite the wealth of in vitro information, fundamental questions about how glutamatergic synapses are formed in the mammalian brain remain unanswered. Glutamate receptor (GluR) delta2 is essential for cerebellar synapse formation in vivo. Here, we show that the N-terminal domain (NTD) of GluRdelta2 interacts with presynaptic neurexins (NRXNs) through cerebellin 1 precursor protein (Cbln1). The synaptogenic activity of GluRdelta2 is abolished in cerebellar primary cultures from Cbln1 knockout mice and is restored by recombinant Cbln1. Knockdown of NRXNs in cerebellar granule cells also hinders the synaptogenic activity of GluRdelta2. Both the NTD of GluRdelta2 and the extracellular domain of NRXN1beta suppressed the synaptogenic activity of Cbln1 in cerebellar primary cultures and in vivo. These results suggest that GluRdelta2 mediates cerebellar synapse formation by interacting with presynaptic NRXNs through Cbln1.

Links

PubMed Online version:10.1016/j.cell.2010.04.035

Keywords

Animals; Cell Line; Cells, Cultured; Cerebellum/metabolism; Humans; Mice; Nerve Tissue Proteins/metabolism; Neural Cell Adhesion Molecules/metabolism; Protein Precursors/metabolism; Receptors, Glutamate/metabolism; Synapses

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:NRX1B

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9R171

F

Seeded From UniProt

complete

MOUSE:GRID2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9R171

F

Seeded From UniProt

complete

MOUSE:CBLN1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0DI97

F

Seeded From UniProt

complete

MOUSE:CBLN1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q61625

F

Seeded From UniProt

complete

MOUSE:CBLN1

involved_in

GO:0021707: cerebellar granule cell differentiation

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q61625

P

Seeded From UniProt

complete

MOUSE:CBLN1

involved_in

GO:0007157: heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q61625

P

Seeded From UniProt

complete

MOUSE:NRX1B

involved_in

GO:0021707: cerebellar granule cell differentiation

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q61625
UniProtKB:Q9R171

P

Seeded From UniProt

complete

MOUSE:NRX1B

involved_in

GO:0007157: heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q61625
UniProtKB:Q9R171

P

Seeded From UniProt

complete

MOUSE:GRID2

involved_in

GO:0007157: heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q9R171

P

Seeded From UniProt

complete

MOUSE:GRID2

involved_in

GO:0021707: cerebellar granule cell differentiation

ECO:0000316: genetic interaction evidence used in manual assertion

UniProtKB:Q9R171

P

Seeded From UniProt

complete


See also

References

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