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首页> 外文期刊>Journal of Cellular Physiology >Proteins of the PDI family: Unpredicted non-ER locations and functions.
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Proteins of the PDI family: Unpredicted non-ER locations and functions.

机译：PDI家族的蛋白质:出乎意料的非急诊的位置和功能。

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摘要

Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. While their functions in the ER have been thoroughly studied, much less is known about their roles in non-ER locations, where, however, they have been shown to be involved in important biological processes. At least three proteins of this family from higher vertebrates have been found in unusual locations (i.e., the cell surface, the extracellular space, the cytosol, and the nucleus), reached through an export mechanism which has not yet been understood. In some cases their function in the non-ER location is clearly related to their redox properties, but in most cases their mechanism of action has still to be disclosed, although their propensity to associate with other proteins or even with DNA might be the main factor responsible for their activities. Copyright 2002 Wiley-Liss, Inc.
机译：蛋白二硫化物异构酶(pdi)构成家庭的结构相关的酶促进二硫键的形成、减少或异构化的新合成的蛋白质内腔的内质网(ER)。因此,行动也陪伴,部分质量控制系统的正确的折叠的蛋白质亚细胞相同隔间。被彻底研究,不太了解然而,他们的角色在非急诊的位置,他们已经被证明参与重要生物过程。这个家庭从高等脊椎动物发现不寻常的位置(即细胞胞质表面,细胞外空间,和原子核),通过一个出口机制尚未清楚。某些情况下,它们的功能在非急诊的位置显然是与它们的氧化还原特性,但在大多数情况下,他们的作用机理透露,尽管他们的倾向与其他蛋白质,甚至与DNA可能会负责他们的主要因素活动。

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