PDI家族蛋白ERp29与凝集素伴侣钙网蛋白形成1:1复合物。
PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin.
作者信息
Sakono Masafumi, Seko Akira, Takeda Yoichi, Ito Yukishige
机构信息
Japan Science and Technology Agency (JST), ERATO, Ito Glycotrilogy Project, 2-1 Hirosawa, Wako, Saitama 351-0198, 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. 2014 Sep 12;452(1):27-31. doi: 10.1016/j.bbrc.2014.08.041. Epub 2014 Aug 15.
Lectin chaperone calreticulin is well known to interact with ERp57 which is one of PDI family proteins. The interaction of ERp57 with calreticulin is believed to assist disulfide bond formation of nascent glycoprotein in the ER. Various kinds of PDI family proteins are present in the ER, however, their precise roles have been unclear. In this study, interaction assay between PDI family proteins and calreticulin by SPR analysis was performed. Our analysis revealed for the first time formation of a 1:1 complex between ERp29 and calreticulin. The dissociation constant of interaction between ERp29 and calreticulin was shown to be almost identical to ERp57-calreticulin interaction. We speculate that the recognition site of ERp29 within calreticulin is different from that of ERp57.
凝集素伴侣钙网蛋白与内质网蛋白57（ERp57）相互作用，ERp57是蛋白质二硫键异构酶（PDI）家族蛋白之一，这是广为人知的。ERp57与钙网蛋白的相互作用被认为有助于内质网中新生糖蛋白二硫键的形成。内质网中存在各种PDI家族蛋白，然而，它们的确切作用尚不清楚。在本研究中，通过表面等离子体共振（SPR）分析进行了PDI家族蛋白与钙网蛋白之间的相互作用测定。我们的分析首次揭示了ERp29与钙网蛋白之间形成了1:1复合物。ERp29与钙网蛋白之间相互作用的解离常数显示与ERp57 - 钙网蛋白相互作用几乎相同。我们推测钙网蛋白内ERp29的识别位点与ERp57的不同。
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