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去唾液酸糖蛋白受体与质膜包被小泡的β衔接蛋白的体外结合

In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles.

作者信息

Beltzer J P, Spiess M

机构信息

Department of Biochemistry, University of Basel, Switzerland.

出版信息

EMBO J. 1991 Dec;10(12):3735-42. doi: 10.1002/j.1460-2075.1991.tb04942.x.

DOI:10.1002/j.1460-2075.1991.tb04942.x
PMID:1935897
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC453108/
Abstract

The asialoglycoprotein (ASGP) receptor was used to probe total clathrin-coated vesicle proteins and purified adaptor proteins (APs) which had been fractionated by gel electrophoresis and transferred to nitrocellulose. The receptor was found to interact with proteins of approximately 100 kDa. The cytoplasmic domain of the ASGP receptor subunit H1 fused to dihydrofolate reductase competed for receptor binding to the 100 kDa polypeptide in the plasma membrane-type AP complexes (AP-2). A fusion protein containing the cytoplasmic domain of the endocytic mutant haemagglutinin HA-Y543 also competed, but a protein with the wild-type haemagglutinin sequence did not. This indicates that the observed interaction is specific for the cytoplasmic domain of the receptor and involves the tyrosine signal for endocytosis. When fractionated by gel electrophoresis in the presence of urea, the ASGP receptor binding polypeptide displayed a characteristic shift in electrophoretic mobility identifying it as the beta adaptin. Partial proteolysis of the AP-2 preparation followed by the receptor binding assay revealed that the aminoterminal domain of the beta adaptin contains the binding site for receptors.

摘要

去唾液酸糖蛋白（ASGP）受体用于探测经凝胶电泳分离并转移至硝酸纤维素膜上的总网格蛋白包被囊泡蛋白和纯化的衔接蛋白（APs）。发现该受体与约100 kDa的蛋白质相互作用。与二氢叶酸还原酶融合的ASGP受体亚基H1的胞质结构域在质膜型AP复合物（AP - 2）中竞争受体与100 kDa多肽的结合。含有内吞突变体血凝素HA - Y543胞质结构域的融合蛋白也能竞争，但具有野生型血凝素序列的蛋白则不能。这表明观察到的相互作用对受体的胞质结构域具有特异性，并且涉及内吞作用的酪氨酸信号。当在尿素存在下进行凝胶电泳分离时，ASGP受体结合多肽在电泳迁移率上呈现出特征性变化，确定其为β衔接蛋白。对AP - 2制剂进行部分蛋白酶解，随后进行受体结合测定，结果表明β衔接蛋白的氨基末端结构域包含受体的结合位点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/e59d2d387ece/emboj00110-0175-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/9239c07a5dc3/emboj00110-0172-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/514d41c601ec/emboj00110-0173-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/ba941ffb6979/emboj00110-0173-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/6835761b2590/emboj00110-0174-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/2da58957dbbf/emboj00110-0175-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/e59d2d387ece/emboj00110-0175-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/9239c07a5dc3/emboj00110-0172-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/514d41c601ec/emboj00110-0173-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/ba941ffb6979/emboj00110-0173-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/6835761b2590/emboj00110-0174-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/2da58957dbbf/emboj00110-0175-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/38f5/453108/e59d2d387ece/emboj00110-0175-b.jpg

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