Abstract:
:The delta2 glutamate receptor (GluRdelta2) has a crucial role in cerebellar functions; disruption of GluRdelta2 alleles in mice (delta2(-/-)) impairs synapse formation and long-term depression, which is thought to underlie motor learning in the cerebellum, and consequently leads to motor discoordination. However, it has been unclear whether GluRdelta2 is activated by glutamate analogues. Here we introduced a GluRdelta2 transgene, which had a mutation (Arg514Lys) in the putative ligand-binding motif conserved in all mammalian ionotropic glutamate receptors (iGluRs) and their ancestral bacterial periplasmic amino-acid-binding proteins, into delta2(-/-) mice. Surprisingly, a mutant GluRdelta2 transgene, as well as a wild-type GluRdelta2 transgene, rescued all abnormal phenotypes of delta2(-/-) mice. Therefore, these results indicate that the conserved arginine residue, which is crucial for the binding of iGluRs to glutamate analogues, is not essential for the restoration of GluRdelta2 functions in delta2(-/-) mice.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Hirai H,Miyazaki T,Kakegawa W,Matsuda S,Mishina M,Watanabe M,Yuzaki Mdoi
10.1038/sj.embor.7400312keywords:
subject
Has Abstractpub_date
2005-01-01 00:00:00pages
90-5issue
1eissn
1469-221Xissn
1469-3178pii
7400312journal_volume
6pub_type
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