WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (30)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Green, W. N.
Right arrow Articles by Wanamaker, C. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Green, W. N.
Right arrow Articles by Wanamaker, C. P.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH

Next Article 

The Journal of Neuroscience, August 1, 1998, 18(15):5555-5564

Formation of the Nicotinic Acetylcholine Receptor Binding Sites

William N. Green and Christian P. Wanamaker

Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, Illinois 60637

Nicotinic acetylcholine receptors (AChRs) are activated by ACh binding to two sites located on different alpha  subunits. The two alpha  subunits, alpha gamma and alpha delta , are distinguished by their interface with gamma  and delta  subunits. We have characterized the formation of the ACh binding sites and found, contrary to the current model, that the sites form at different times and in a set order. The first site forms on alpha gamma subunits during the process of subunit assembly. Our data are consistent with the appearance of this site on alpha beta gamma delta subunit tetramers soon after the site for the competitive antagonist alpha -bungarotoxin has formed and delta  subunits have assembled with alpha beta gamma trimers. The second site is located on alpha delta subunits and forms after AChR subunits have assembled into alpha 2beta gamma delta pentamers. By determining the order in which the ACh binding sites form, we have also identified the sites in which the delta  and second alpha subunits associate during subunit assembly.

Key words: protein folding and assembly; acetylcholine; alpha -bungarotoxin; nicotinic receptors; pharmacology; ligand binding sites


Copyright © 1998 Society for Neuroscience  0270-6474/98/18155555-10$05.00/0


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
C. P. Wanamaker and W. N. Green
Endoplasmic Reticulum Chaperones Stabilize Nicotinic Receptor Subunits and Regulate Receptor Assembly
J. Biol. Chem., October 26, 2007; 282(43): 31113 - 31123.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. P. Wanamaker and W. N. Green
N-Linked Glycosylation Is Required for Nicotinic Receptor Assembly but Not for Subunit Associations with Calnexin
J. Biol. Chem., October 7, 2005; 280(40): 33800 - 33810.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
R. C. Drisdel, E. Manzana, and W. N. Green
The Role of Palmitoylation in Functional Expression of Nicotinic {alpha}7 Receptors
J. Neurosci., November 17, 2004; 24(46): 10502 - 10510.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Psaridi-Linardaki, A. Mamalaki, M. Remoundos, and S. J. Tzartos
Expression of Soluble Ligand- and Antibody-binding Extracellular Domain of Human Muscle Acetylcholine Receptor alpha Subunit in Yeast Pichia pastoris. ROLE OF GLYCOSYLATION IN alpha -BUNGAROTOXIN BINDING
J. Biol. Chem., July 19, 2002; 277(30): 26980 - 26986.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
M. Mitra, C. P. Wanamaker, and W. N. Green
Rearrangement of Nicotinic Receptor {alpha} Subunits during Formation of the Ligand Binding Sites
J. Neurosci., May 1, 2001; 21(9): 3000 - 3008.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. T. Dineley and J. W. Patrick
Amino Acid Determinants of alpha 7 Nicotinic Acetylcholine Receptor Surface Expression
J. Biol. Chem., April 28, 2000; 275(18): 13974 - 13985.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
P. M. Taylor, C. N. Connolly, J. T. Kittler, G. H. Gorrie, A. Hosie, T. G. Smart, and S. J. Moss
Identification of Residues within GABAA Receptor alpha Subunits That Mediate Specific Assembly with Receptor beta Subunits
J. Neurosci., February 15, 2000; 20(4): 1297 - 1306.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Kuusinen, R. Abele, D. R. Madden, and K. Keinanen
Oligomerization and Ligand-binding Properties of the Ectodomain of the alpha -Amino-3-hydroxy-5-methyl-4-isoxazole Propionic Acid Receptor Subunit GluRD
J. Biol. Chem., October 8, 1999; 274(41): 28937 - 28943.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
A. L. Eertmoed and W. N. Green
Nicotinic Receptor Assembly Requires Multiple Regions throughout the gamma Subunit
J. Neurosci., August 1, 1999; 19(15): 6298 - 6308.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
V. K. Ramanathan and Z. W. Hall
Altered Glycosylation Sites of the delta Subunit of the Acetylcholine Receptor (AChR) Reduce alpha delta Association and Receptor Assembly
J. Biol. Chem., July 16, 1999; 274(29): 20513 - 20520.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
W. N. Green
Ion Channel Assembly: Creating Structures that Function
J. Gen. Physiol., February 1, 1999; 113(2): 163 - 170.
[Full Text] [PDF]


Home page
JGPHome page
S. H. Keller and P. Taylor
Determinants Responsible for Assembly of the Nicotinic Acetylcholine Receptor
J. Gen. Physiol., February 1, 1999; 113(2): 171 - 176.
[Full Text] [PDF]



-
-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2009 by Society for Neuroscience ONLINE ISSN: 1529-2401
-