| The proximal and distal C-terminal tail domains of the CB1 cannabinoid receptor mediate G protein coupling. | |
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MedLine Citation:
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PMID: 11744255 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The human CB1 cannabinoid receptor couples to G(i/o) proteins and inhibits neuronal voltage-gated Ca2+ channels. The role of the C-terminal tail of the CB1 cannabinoid receptor in G(i/o) protein coupling was examined using the superior cervical ganglion neuronal expression system. Deletion of the distal intracellular C-terminal tail (amino acids 418-472) slowed the kinetics and reduced the magnitude of Ca2+ channel inhibition. Deletion of the entire intracellular C-terminal tail (amino acids 401-472) abolished Ca2+ channel inhibition demonstrating the critical role of the proximal amino acids 401-417 of the C-terminal tail in G protein signaling. Expression of the C-terminal truncated receptors on the cell surface was examined using an N-terminal CB1 antibody. Both the C-terminal truncated receptors were expressed on the cell surface and were no different from wild type CB1 cannabinoid receptors. This study establishes that the proximal CB1 cannabinoid receptor intracellular C-terminal tail domain (amino acids 401-417) is critical for G(i/o) protein coupling and that the distal C-terminal tail domain (amino acids 418-472) profoundly modulates both the magnitude and kinetics of signal transduction. Thus, the C-terminal tail of the CB1 cannabinoid receptor has a wider role in G protein coupling than was previously thought. |
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Authors:
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J Nie; D L Lewis |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Neuroscience Volume: 107 ISSN: 0306-4522 ISO Abbreviation: Neuroscience Publication Date: 2001 |
Date Detail:
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Created Date: 2001-12-17 Completed Date: 2002-02-01 Revised Date: 2009-11-03 |
Medline Journal Info:
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Nlm Unique ID: 7605074 Medline TA: Neuroscience Country: United States |
Other Details:
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Languages: eng Pagination: 161-7 Citation Subset: IM |
Affiliation:
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Department of Pharmacology and Toxicology, Medical College of Georgia, Room CB3515, 1120 15th Street, Augusta, GA 30912-2300, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence
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genetics Animals Brain / drug effects, metabolism* Calcium Channels / metabolism* Cells, Cultured DNA, Complementary / genetics, pharmacology GTP-Binding Proteins / metabolism* Genetic Vectors Male Neurons / drug effects, metabolism* Peptide Fragments / genetics, metabolism Protein Structure, Tertiary / physiology Protein Transport / genetics Rats Rats, Wistar Receptors, Cannabinoid Receptors, Cell Surface / genetics, metabolism* Receptors, Drug / drug effects, genetics, metabolism* Signal Transduction / physiology* |
| Grant Support | |
ID/Acronym/Agency:
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DA00286/DA/NIDA NIH HHS; DA11322/DA/NIDA NIH HHS; R01 DA10350/DA/NIDA NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Calcium Channels; 0/DNA, Complementary; 0/Peptide Fragments; 0/Receptors, Cannabinoid; 0/Receptors, Cell Surface; 0/Receptors, Drug; EC 3.6.1.-/GTP-Binding Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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