Document Detail


The first and third intracellular loops together with the carboxy terminal tail of the delta-opioid receptor contribute toward functional interaction with Galpha16.
MedLine Citation:
PMID:  14535952     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Opioid peptides exert their regulatory effects on both central and peripheral nervous systems via multiple opioid receptors that are linked to seemingly identical sets of guanine nucleotide-binding regulatory proteins (G proteins). In contrast to the mu-opioid receptor, the delta-opioid receptor can efficiently stimulate phospholipase C via G16. We used a series of mu/delta-opioid receptor chimeras to examine the involvement of intracellular receptor domains in the recognition of G16. After ascertaining that the chimeras can bind opioid ligands with high affinity and elicit inhibition of adenylyl cyclase, COS-7 cells were cotransfected with cDNAs encoding Galpha16 and a mu/delta-opioid receptor chimera and assayed for [D-Ala2,D-Leu5]enkephalin-induced stimulation of phospholipase C. Our results indicate that (i) the carboxy terminal tail of the delta-opioid receptor is necessary but insufficient for conferring coupling to Galpha16, (ii) the third inner loop together with the carboxy terminal tail of the delta-opioid receptor can provide sufficient contact domains for Galpha16, and (iii) the first inner loop of the delta-opioid receptor, in particular Leu80, as well as the fifth transmembrane domain and/or the third extracellular loop may also contribute in defining the fidelity of interaction between the delta-opioid receptor and Galpha16. These results indicate that efficient coupling of the delta-opioid receptor to Galpha16 requires the participation of most of the intracellular regions, including the first intracellular loop.
Authors:
Anthony S L Chan; Ping Y Law; Horace H Loh; Peter N N Ho; Wai-Man Wu; Joy S C Chan; Yung H Wong
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of neurochemistry     Volume:  87     ISSN:  0022-3042     ISO Abbreviation:  J. Neurochem.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-10-10     Completed Date:  2003-11-24     Revised Date:  2012-07-12    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  England    
Other Details:
Languages:  eng     Pagination:  697-708     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Hong Kong University of Science and Technology, Kowloon, Hong Kong, China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
COS Cells
Enkephalin, Leucine-2-Alanine / pharmacology
GTP-Binding Protein alpha Subunits, Gq-G11
Heterotrimeric GTP-Binding Proteins / genetics,  metabolism*
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Binding / genetics,  physiology
Protein Structure, Tertiary / physiology
Rats
Receptors, Opioid, delta / genetics,  metabolism*
Receptors, Opioid, mu / genetics,  metabolism
Recombinant Fusion Proteins / genetics,  metabolism
Sequence Homology, Amino Acid
Structure-Activity Relationship
Transfection
Type C Phospholipases / drug effects,  metabolism
Chemical
Reg. No./Substance:
0/Receptors, Opioid, delta; 0/Receptors, Opioid, mu; 0/Recombinant Fusion Proteins; 63631-40-3/Enkephalin, Leucine-2-Alanine; EC 3.1.4.-/Type C Phospholipases; EC 3.6.5.1/G protein alpha 16; EC 3.6.5.1/GTP-Binding Protein alpha Subunits, Gq-G11; EC 3.6.5.1/Heterotrimeric GTP-Binding Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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