PDI家族蛋白ERp29识别分子伴侣钙连蛋白的P结构域。

PDI family protein ERp29 recognizes P-domain of molecular chaperone calnexin.

作者信息

Nakao Hitomi, Seko Akira, Ito Yukishige, Sakono Masafumi

机构信息

Department of Applied Chemistry, University of Toyama, 3190 Gofuku, Toyama, Toyama 930-855, Japan.

Japan Science and Technology Agency (JST), ERATO Ito Glycotrilogy Project, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

出版信息

Biochem Biophys Res Commun. 2017 Jun 3;487(3):763-767. doi: 10.1016/j.bbrc.2017.04.139. Epub 2017 Apr 26.

DOI:10.1016/j.bbrc.2017.04.139

PMID:28456374

Abstract

Endoplasmic reticulum (ER) resident lectin chaperone calnexin (CNX) and calreticulin (CRT) assist folding of nascent glycoproteins. Their association with ERp57, a member of PDI family proteins (PDIs) which promote disulfide bond formation of unfolded proteins, has been well documented. Recent studies have provided evidence that other PDIs may also interact with CNX and CRT. Accordingly, it seems possible that the ER provides a repertoire of CNX/CRT-PDI complexes, in order to facilitate refolding of various glycoproteins. In this study, we examined the ability of PDIs to interact with CNX. Among them ERp29 was shown to interact with CNX, similarly to ERp57. Judging from the dissociation constant, its ability to interact with CNX was similar to that of ERp57. Results of further analyses by using a CNX mutant imply that ERp29 and ERp57 recognize the same domain of CNX, whereas the mode of interaction with CNX might be somewhat different between them.

摘要

内质网（ER）驻留凝集素伴侣钙连蛋白（CNX）和钙网蛋白（CRT）协助新生糖蛋白的折叠。它们与ERp57的关联已有充分记载，ERp57是促进未折叠蛋白二硫键形成的蛋白质二硫键异构酶（PDI）家族蛋白的一员。最近的研究表明，其他PDI也可能与CNX和CRT相互作用。因此，内质网似乎有可能提供一系列CNX/CRT-PDI复合物，以促进各种糖蛋白的重新折叠。在本研究中，我们检测了PDI与CNX相互作用的能力。其中，ERp29被证明与CNX相互作用，类似于ERp57。从解离常数判断，其与CNX相互作用的能力与ERp57相似。使用CNX突变体进行的进一步分析结果表明，ERp29和ERp57识别CNX的相同结构域，而它们与CNX的相互作用模式可能略有不同。