ACETYLCHOLINE-RECEPTOR ASSEMBLY - SUBUNIT FOLDING AND OLIGOMERIZATION OCCUR SEQUENTIALLY
ACETYLCHOLINE-RECEPTOR ASSEMBLY - SUBUNIT FOLDING AND OLIGOMERIZATION OCCUR SEQUENTIALLY
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DOI：
10.1016/0092-8674(93)90294-z
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发表时间：
1993-07-16
期刊：
影响因子：
64.5
通讯作者：
CLAUDIO, T
中科院分区：
文献类型：
--
作者：
GREEN, WN;CLAUDIO, T
本文研究了T. calfornica用于鉴定AChR亚基折叠和寡聚化的步骤。通过降低至组装允许温度来分离组装中间体。最早可识别的组装中间体，α-γ-三聚体，在亚基合成后几分钟形成。通过将δ亚基添加到三聚体中缓慢形成α-β-γ-δ四聚体，最后添加第二个α亚基形成α-2 β-γ-δ五聚体。在这些寡聚化步骤之间，通过α-银环蛇毒素结合位点形成、抗原表位的出现、表观分子量的变化和去污剂溶解度的变化监测亚基折叠。亚基折叠需要亚基的特定组合，并与亚基添加时间相关，表明这些亚基折叠事件有助于组装过程中亚基识别位点的形成。
The temperature sensitivity of nicotinic acetylcholine receptors (AChRs) from T. californica was used to identify steps in AChR subunit folding and oligomerization. Assembly intermediates were isolated by lowering to an assembly-permissive temperature. The earliest identifiable assembly intermediates, alphabetagamma trimers, form minutes after subunit synthesis. Alphabetagammadelta tetramers are formed slowly by the addition of delta subunits to trimers, and finally a second alpha subunit is added to form alpha2betagammadelta pentamers. Between these oligomerization steps, subunits fold as monitored by alpha-bungarotoxin-binding site formation, appearance of antigenic epitopes, changes in apparent molecular weight, and changes in detergent solubility. Subunit folding requires specific combinations of subunits and correlates in time with subunit additions, suggesting that these subunit folding events contribute to subunit recognition site formation during assembly.