Functional Coupling of a Human Retinal Metabotropic Glutamate Receptor (hmGluR6) to Bovine Rod Transducin and Rat Go in an in Vitro Reconstitution System

The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS cell membranes using an antibody affinity column. The purified receptor was then reconstituted into lipid vesicles, and its ability to activ...

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Published inThe Journal of biological chemistry Vol. 272; no. 52; pp. 33100 - 33104
Main Authors Weng, Ke, Lu, C.-C., Daggett, Lorrie P., Kuhn, Rainer, Flor, Peter J., Johnson, Edwin C., Robinson, Phyllis R.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 26.12.1997
American Society for Biochemistry and Molecular Biology
Subjects
Amino Acid Sequence
Aminobutyrates - pharmacology
Animals
Anticonvulsants - pharmacology
Cattle
COS Cells
Excitatory Amino Acid Agonists - pharmacology
GTP-Binding Protein alpha Subunits, Gi-Go
GTP-Binding Proteins - metabolism
Guanosine 5'-O-(3-Thiotriphosphate) - metabolism
Guanosine Triphosphate - metabolism
Humans
Molecular Sequence Data
Rats
Receptors, Metabotropic Glutamate - genetics
Receptors, Metabotropic Glutamate - metabolism
Transducin - metabolism
Transfection
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Abstract The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS cell membranes using an antibody affinity column. The purified receptor was then reconstituted into lipid vesicles, and its ability to activate either transducin, the rod photoreceptor-specific GTP-binding protein, or the α subunit of Go was assayed in vitro using a guanosine 5′-3-O-(thio)triphosphate binding assay. Activation of both transducin and Go was observed. The rate of Goactivation was 18-fold greater than the rate of transducin activation. This indicates that the coupling of mGluR6 to Go is more efficient and suggests that Go may be involved in coupling to mGluR6 in ON-bipolar cells.
AbstractList The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS cell membranes using an antibody affinity column. The purified receptor was then reconstituted into lipid vesicles, and its ability to activate either transducin, the rod photoreceptor-specific GTP-binding protein, or the alpha subunit of Go was assayed in vitro using a guanosine 5'-3-O-(thio)triphosphate binding assay. Activation of both transducin and Go was observed. The rate of Go activation was 18-fold greater than the rate of transducin activation. This indicates that the coupling of mGluR6 to Go is more efficient and suggests that Go may be involved in coupling to mGluR6 in ON-bipolar cells.
The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS cell membranes using an antibody affinity column. The purified receptor was then reconstituted into lipid vesicles, and its ability to activate either transducin, the rod photoreceptor-specific GTP-binding protein, or the α subunit of G o was assayed in vitro using a guanosine 5′-3- O -(thio)triphosphate binding assay. Activation of both transducin and G o was observed. The rate of G o activation was 18-fold greater than the rate of transducin activation. This indicates that the coupling of mGluR6 to G o is more efficient and suggests that G o may be involved in coupling to mGluR6 in ON-bipolar cells.
The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS cell membranes using an antibody affinity column. The purified receptor was then reconstituted into lipid vesicles, and its ability to activate either transducin, the rod photoreceptor-specific GTP-binding protein, or the α subunit of Go was assayed in vitro using a guanosine 5′-3-O-(thio)triphosphate binding assay. Activation of both transducin and Go was observed. The rate of Goactivation was 18-fold greater than the rate of transducin activation. This indicates that the coupling of mGluR6 to Go is more efficient and suggests that Go may be involved in coupling to mGluR6 in ON-bipolar cells.
Author Johnson, Edwin C.
Weng, Ke
Flor, Peter J.
Kuhn, Rainer
Robinson, Phyllis R.
Daggett, Lorrie P.
Lu, C.-C.
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  organization: Department of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland 21250
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Snippet The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS...
The cDNA encoding hmGluR6, appended with a 15-amino acid antibody epitope (1D4), was transiently transfected in COS-7 cells. The receptor was purified from COS...
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elsevier
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StartPage 33100
SubjectTerms Amino Acid Sequence
Aminobutyrates - pharmacology
Animals
Anticonvulsants - pharmacology
Cattle
COS Cells
Excitatory Amino Acid Agonists - pharmacology
GTP-Binding Protein alpha Subunits, Gi-Go
GTP-Binding Proteins - metabolism
Guanosine 5'-O-(3-Thiotriphosphate) - metabolism
Guanosine Triphosphate - metabolism
Humans
Molecular Sequence Data
Rats
Receptors, Metabotropic Glutamate - genetics
Receptors, Metabotropic Glutamate - metabolism
Transducin - metabolism
Transfection
Title Functional Coupling of a Human Retinal Metabotropic Glutamate Receptor (hmGluR6) to Bovine Rod Transducin and Rat Go in an in Vitro Reconstitution System
URI https://dx.doi.org/10.1074/jbc.272.52.33100
http://www.jbc.org/content/272/52/33100.abstract
https://www.ncbi.nlm.nih.gov/pubmed/9407094
https://search.proquest.com/docview/79484343
Volume 272
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