Mapping of the Mouse Glutamate Receptor δ1Subunit (Grid1) to Chromosome 14

Treadaway, Jason; Zuo, Jian

doi:10.1006/geno.1998.5599

Cited by 5 publications

(3 citation statements)

References 5 publications

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“…These findings provide the first in vivo evidence of a functional role for this largely uncharacterized orphan glutamate receptor, which is consistent with its prominent inner ear expression. Given the prevalence of congenital or acquired high-frequency hearing loss in human ears, the locus encoding GluR␦1 represents a candidate disease gene (39).…”

Section: Discussionmentioning

confidence: 99%

Orphan Glutamate Receptor δ1 Subunit Required for High-Frequency Hearing

Gao

Maison

et al. 2007

Molecular and Cellular Biology

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The function of the orphan glutamate receptor delta subunits (GluR␦1 and GluR␦2) remains unclear. GluR␦2 is expressed exclusively in the Purkinje cells of the cerebellum, and GluR␦1 is prominently expressed in inner ear hair cells and neurons of the hippocampus. We found that mice lacking the GluR␦1 protein displayed significant cochlear threshold shifts for frequencies of >16 kHz. These deficits correlated with a substantial loss of type IV spiral ligament fibrocytes and a significant reduction of endolymphatic potential in high-frequency cochlear regions. Vulnerability to acoustic injury was significantly enhanced; however, the efferent innervation of hair cells and the classic efferent inhibition of outer hair cells were unaffected. Hippocampal and vestibular morphology and function were normal. Our findings show that the orphan GluR␦1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea, and the locus encoding GluR␦1 represents a candidate gene for congenital or acquired high-frequency hearing loss in humans.

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Section: Discussionmentioning

confidence: 99%

Orphan Glutamate Receptor δ1 Subunit Required for High-Frequency Hearing

Gao

Maison

et al. 2007

Molecular and Cellular Biology

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“…We took advantage of an established gene mapping panel, the Jackson BSS backcross (Rowe et al, 1994), that consists of 94 offspring of a backcross between two distantly related mouse strains, Mus musculus (C57BL/6) and M. spretus. First, a DNA polymorphism was identified in the 3Ј UTR of the cbln3 gene using single-strand conformation polymorphism between the two strains (Treadaway and Zuo, 1998). Subsequently, we determined the pattern of segregation of the two strains at the cbln3 locus in the Jackson BSS panel.…”

Section: Genomic Structure and Chromosomal Location Of Cbln3mentioning

confidence: 99%

Cbln3, a Novel Member of the Precerebellin Family that Binds Specifically to Cbln1

2000

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Precerebellin (Cbln1) is the precursor of the brain-specific hexadecapeptide cerebellin. Although cerebellin has properties of a conventional neuropeptide, its function is controversial because Cbln1 has structural features characteristic of circulating atypical collagens. Cbln1 is related to the three subunits of the complement C1q complex. Therefore, we hypothesized that Cbln1 participated in analogous heteromeric complexes with precerebellin-related proteins. Using LexA-Cbln1 as bait in a yeast two-hybrid screen, we isolated a cDNA encoding a novel Cbln1-related protein, designated Cbln3. The gene encoding cbln3 had the same intron-exon structure as cbln1 but mapped to a different mouse chromosome (14). The deduced amino acid sequence of Cbln3 was 55% identical to Cbln1 and also contained a C1q signature domain and signal sequence for secretion. In addition to binding avidly to Cbln3, Cbln1 also formed homomeric complexes. In contrast, Cbln3 homomeric association was weak. These interactions exhibited specificity because C1qB bound to neither Cbln1 nor Cbln3. Like cbln1, cbln3 was expressed in the cerebellum and dorsal cochlear nucleus in which it was detected in granule neurons. Because Cbln1 and Cbln3 are coexpressed in the brain and interact avidly, they may function as a secreted heteromeric complex in vivo.

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“…Therefore, besides compiling the available data on the two subunits, the present review attempts to look at both delta receptors from an 'ion [55,[62][63][64]. Comparable gene structure and sizes are found in rat and mouse [55].…”

Section: Introductionmentioning

confidence: 96%

To Gate or not to Gate: Are the Delta Subunits in the Glutamate Receptor Family Functional Ion Channels?

Schmid

Hollmann

2008

Mol Neurobiol

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The two delta receptor subunits remain the most puzzling enigma within the ionotropic glutamate receptor family. Despite the recent elucidation of the ligand-binding domain structure of delta2, many fundamental questions with regard to the subunits' mechanism of function still remain unanswered. Of necessity, the majority of studies on delta receptors focused on the metabotropic function of delta2, since electrophysiological approaches to date are limited to the characterization of spontaneous currents through the delta2-lurcher mutant. Indeed, accumulated evidence primarily from delta2-deficient transgenic mice suggest that major physiological roles of delta2 are mediated via metabotropic signaling by the subunit's C terminus. Why then would the subunits retain a conserved ion channel domain if they do not form functional ion channels? Any progress with regard to ionotropic function of the two delta subunits has been hampered by their largely unknown pharmacology. Even now that a pharmacological profile for delta2 is being established on the basis of the ligand-binding domain structure, wild-type delta2 channels in heterologous expression systems stay closed in the presence of molecules that have been demonstrated to bind to the receptor's ligand-binding domain. In this paper, we review the current knowledge of delta subunits focusing on the disputed ionotropic function.

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Mapping of the Mouse Glutamate Receptor δ1Subunit (Grid1) to Chromosome 14

Cited by 5 publications

References 5 publications

Orphan Glutamate Receptor δ1 Subunit Required for High-Frequency Hearing

Orphan Glutamate Receptor δ1 Subunit Required for High-Frequency Hearing

Cbln3, a Novel Member of the Precerebellin Family that Binds Specifically to Cbln1

To Gate or not to Gate: Are the Delta Subunits in the Glutamate Receptor Family Functional Ion Channels?

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