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The amino-terminal domain of glutamate receptor {delta}2 triggers presynaptic differentiation

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [1]
  1. Department of Molecular Neurobiology and Pharmacology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033 (Japan)
Glutamate receptor (GluR) {delta}2 selectively expressed in cerebellar Purkinje cells plays key roles in synapse formation, long-term depression and motor learning. We propose that GluR{delta}2 regulates synapse formation by making a physical linkage between the active zone and postsynaptic density. To examine the issue, GluR{delta}2-transfected 293T cells were cultured with cerebellar neurons. We found numerous punctate signals for presynaptic markers on the surface of 293T cells expressing GluR{delta}2. The presynaptic specializations induced by GluR{delta}2 were capable of exo- and endocytosis as indicated by FM1-43 dye labeling. Replacement of the extracellular N-terminal domain (NTD) of GluR{delta}2 with that of the AMPA receptor GluR{alpha}1 abolished the inducing activity. The NTD of GluR{delta}2 fused to the immunoglobulin constant region successfully induced the accumulation of presynaptic specializations on the surface of beads bearing the fusion protein. These results suggest that GluR{delta}2 triggers presynaptic differentiation by direct interaction with presynaptic components through the NTD.
OSTI ID:
21255816
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 4 Vol. 377; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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