STRUCTURAL AND FUNCTIONAL DIVISION INTO 2 DOMAINS OF THE LARGE (100-KDA TO 115-KDA) CHAINS OF THE CLATHRIN-ASSOCIATED PROTEIN COMPLEX AP-2
STRUCTURAL AND FUNCTIONAL DIVISION INTO 2 DOMAINS OF THE LARGE (100-KDA TO 115-KDA) CHAINS OF THE CLATHRIN-ASSOCIATED PROTEIN COMPLEX AP-2
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DOI：
10.1073/pnas.86.8.2612
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发表时间：
1989-04-01
影响因子：
11.1
通讯作者：
DAVIS, AE
中科院分区：
文献类型：
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作者：
KIRCHHAUSEN, T;NATHANSON, KL;DAVIS, AE
网格蛋白相关蛋白复合物2（AP-2复合物）是一组与网格蛋白包被的囊泡相关的蛋白质，据信与质膜中发现的受体的胞质结构域相互作用。将AP-2纯化为几条多肽链的组装体（α，β，AP 50和AP 17），其中只有α.和β链（100-115 kDa）显示出显著的异质性。我们已经获得了两种不同的大鼠脑β的cDNA克隆。店我们还研究了牛脑AP-2复合物的结构域组织的选择性蛋白水解。这些研究的结果表明，和β链也有类似的两域组织。它们的氨基末端结构域相对不变，而它们的羧基末端结构域在序列和长度上都是可变的。我们建议，可变结构域选择受体包被囊泡。
The clathrin-associated protein complex 2 (AP-2 complex) is a group of proteins associated with clathrin-coated vesicles and believed to interact with cytoplasmic domains of receptors found in the plasma membrane. AP-2 was purified as an assembly of several polypeptide chains (.alpha., .beta., AP50, and AP17), of which only the .alpha. and .beta. chains (100-115 kDa) show significant heterogeneity. We have obtained cDNA clones for two distinct rat brain .beta. chains. We have also studied the domain organization of bovine brain AP-2 complexes by selective proteolysis. Results of these studies show that the .alpha. and .beta. chains have a similar two-domain organization. Their amino-terminal domains are relatively invariant whereas their carboxyl-terminal domains are variable in both sequence and length. We propose that the variable domains select receptors for inclusion in coated vesicles.