ROLE OF 2 ACETYLCHOLINE-RECEPTOR SUBUNIT DOMAINS IN HOMOMER FORMATION AND INTERSUBUNIT RECOGNITION, AS REVEALED BY ALPHA-3 AND ALPHA-7 SUBUNIT CHIMERAS

被引:50
作者
GARCIAGUZMAN, M
SALA, F
SALA, S
CAMPOSCARO, A
CRIADO, M
机构
[1] UNIV ALICANTE,DEPT NEUROCHEM,E-03080 ALACANT,SPAIN
[2] UNIV ALICANTE,DEPT PHARMACOL,E-03080 ALACANT,SPAIN
[3] UNIV ALICANTE,DEPT PHYSIOL,E-03080 ALACANT,SPAIN
[4] UNIV ALICANTE,INST NEUROSCI,E-03080 ALACANT,SPAIN
关键词
D O I
10.1021/bi00254a031
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Differential expression of subunit genes from the nicotinic acetylcholine receptor (AChR) superfamily yields distinct receptor subtypes. As each AChR subtype has a specific subunit composition and many subunit combinations appear not to be expressed, each subunit must contain some information leading to proper assembly. The neuronal AChR subunits alpha 3 and alpha 7 are expressed in bovine chromaffin cells, probably as constituents of two different AChR subtypes. These subunits have different assembly behavior when expressed in heterologous expression systems: alpha 7 subunits are able to produce homomeric AChRs, whereas alpha 3 subunits require other ''structural'' subunits for functional expression of AChRs. This feature allows the dissection of the requirements for subunit interactions during AChR formation. Analysis of alpha 7/alpha 3 chimeric constructs identified two regions essential to homomeric assembly and intersubunit recognition: an N-terminal extracellular region, controlling the initial association between subunits, and a second domain within a region comprising the first putative transmembrane segment, M1, and the cytoplasmic loop coupling it to the pore-forming segment, M2, involved in the subsequent interaction and stabilization of the oligomeric complex.
引用
收藏
页码:15198 / 15203
页数:6
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