一组伴侣蛋白和折叠酶在内质网中形成多蛋白复合物，结合新生蛋白。
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Meunier L, Usherwood YK, Chung KT, Hendershot LM
一组伴侣蛋白和折叠酶在内质网中形成多蛋白复合物，结合新生蛋白。
Mol Biol Cell, 2002 12月;13(12):4456-69。
- PubMed ID
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12475965 (PubMed视图］
- 摘要
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我们证明了存在一个大的内质网(ER)定位的多蛋白复合体，它由分子伴侣BiP组成;GRP94;CaBP1;蛋白质二硫异构酶(PDI);ERdj3，最近发现的ER Hsp40共伴侣;还有B;ERp72;GRP170;UDP-glucosyltransferase;和SDF2-L1。 This complex is associated with unassembled, incompletely folded immunoglobulin heavy chains. Except for ERdj3, and to a lesser extent PDI, this complex also forms in the absence of nascent protein synthesis and is found in a variety of cell types. Cross-linking studies reveal that the majority of these chaperones are included in the complex. Our data suggest that this subset of ER chaperones forms an ER network that can bind to unfolded protein substrates instead of existing as free pools that assembled onto substrate proteins. It is noticeable that most of the components of the calnexin/calreticulin system, which include some of the most abundant chaperones inside the ER, are either not detected in this complex or only very poorly represented. This study demonstrates an organization of ER chaperones and folding enzymes that has not been previously appreciated and suggests a spatial separation of the two chaperone systems that may account for the temporal interactions observed in other studies.