scholarly journals Asymmetric distribution of dystrophin in developing and adult Torpedo marmorata electrocyte: evidence for its association with the acetylcholine receptor-rich membrane.

1990 ◽  
Vol 87 (10) ◽  
pp. 3938-3941 ◽  
Author(s):  
B. J. Jasmin ◽  
A. Cartaud ◽  
M. A. Ludosky ◽  
J. P. Changeux ◽  
J. Cartaud
1989 ◽  
Vol 108 (1) ◽  
pp. 127-139 ◽  
Author(s):  
E Kordeli ◽  
J Cartaud ◽  
H O Nghiêm ◽  
A Devillers-Thiéry ◽  
J P Changeux

The assembly of the nicotinic acetylcholine receptor (AchR) and the 43-kD protein (v1), the two major components of the post synaptic membrane of the electromotor synapse, was followed in Torpedo marmorata electrocyte during embryonic development by immunocytochemical methods. At the first developmental stage investigated (45-mm embryos), accumulation of AchR at the ventral pole of the newly formed electrocyte was observed within columns before innervation could be detected. No concomitant accumulation of 43-kD immunoreactivity in AchR-rich membrane domains was observed at this stage, but a transient asymmetric distribution of the extracellular protein, laminin, which paralleled that of the AchR, was noticed. At the subsequent stage studied (80-mm embryos), codistribution of the two proteins was noticed on the ventral face of the cell. Intracellular pools of AchR and 43-kD protein were followed at the EM level in 80-mm electrocytes. AchR immunoreactivity was detected within membrane compartments, which include the perinuclear cisternae of the endoplasmic reticulum and the plasma membrane. On the other hand, 43-kD immunoreactivity was not found associated with the AchR in the intracellular compartments of the cell, but codistributed with the AchR at the level of the plasma membrane. The data reported in this study suggest that AchR clustering in vivo is not initially determined by the association of the AchR with the 43-kD protein, but rather relies on AchR interaction with extracellular components, for instance from the basement membrane, laid down in the tissue before the entry of the electromotor nerve endings.


1984 ◽  
Vol 99 (4) ◽  
pp. 1202-1211 ◽  
Author(s):  
A Brisson ◽  
P N Unwin

Well-ordered tubular crystals of acetylcholine receptor were obtained from suspensions of Torpedo marmorata receptor-rich vesicles. They are composed of pairs of oppositely oriented molecules arranged on the surface lattice with the symmetry of the plane group p2 (average unit cell dimensions: a = 90 A, b = 162 A, gamma = 117 degrees). The receptor in this lattice has an asymmetric distribution of mass around its perimeter, yet a regular pentagonal shape; thus its five transmembrane subunits appear to have different lengths, but approximately equal cross sections. The tubes grow by lateral aggregation on the vesicle surface of ribbons of the paired molecules. Both ribbons and tubes were sensitive to dispersal by the disulphide reductant, dithiothreitol. This observation and other evidence suggest that the basic pairing interaction in the tubes may be that of the physiological dimer, involving contact between delta-subunits.


FEBS Letters ◽  
1980 ◽  
Vol 121 (2) ◽  
pp. 327-332 ◽  
Author(s):  
Jean Cartaud ◽  
Jean-Luc Popot ◽  
Jean-Pierre Changeux

1982 ◽  
Vol 1 (6) ◽  
pp. 713-717 ◽  
Author(s):  
J. Giraudat ◽  
A. Devillers-Thiery ◽  
C. Auffray ◽  
F. Rougeon ◽  
J.P. Changeux

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