Document Detail


Nicotinic receptor assembly requires multiple regions throughout the gamma subunit.
MedLine Citation:
PMID:  10414959     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Assembly of ionotropic neurotransmitter receptors typified by acetylcholine receptors (AChRs) is thought to be directed by an N-terminal extracellular domain of a subunit. Consistent with this hypothesis, chimeras with the delta subunit N-terminal domain fused to the rest of the gamma subunit can substitute for delta, but not gamma, subunits during AChR assembly. However, chimeras with the gamma subunit N-terminal domain fused to the rest of the delta subunit cannot substitute for gamma or delta subunits during assembly. Furthermore, expression of this chimera with the four wild-type subunits prevents the formation of alpha-bungarotoxin (Bgt) binding sites. Instead of AChR pentamers, complexes are assembled containing only the chimera and either alpha or beta subunits. Based on the results of additional gamma-delta chimeras, there are at least two different regions within the C-terminal half of the chimera required for the dominant-negative effect. Our results indicate that the N-terminal domain of the gamma subunit mediates the initial subunit associations, whereas signals in the C-terminal half of the subunit are required for subsequent subunit interactions.
Authors:
A L Eertmoed; W N Green
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of neuroscience : the official journal of the Society for Neuroscience     Volume:  19     ISSN:  0270-6474     ISO Abbreviation:  J. Neurosci.     Publication Date:  1999 Aug 
Date Detail:
Created Date:  1999-08-16     Completed Date:  1999-08-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8102140     Medline TA:  J Neurosci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6298-308     Citation Subset:  IM    
Affiliation:
Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, Illinois 60637, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites / physiology
Bungarotoxins / metabolism
Cell Line
Chimera / genetics,  physiology
Peptide Fragments / genetics
Protein Isoforms / genetics
Protein Processing, Post-Translational*
Receptors, Nicotinic / genetics,  physiology*
Signal Transduction / physiology
Torpedo
Chemical
Reg. No./Substance:
0/Bungarotoxins; 0/Peptide Fragments; 0/Protein Isoforms; 0/Receptors, Nicotinic

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


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