Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2R3, Canada.
School of Human Nutrition, McGill University, Sainte Anne de Bellevue, QC H9X 3V9, Canada.
Cells. 2023 Jan 24;12(3):403. doi: 10.3390/cells12030403.
Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in the folding and quality control of membrane-associated and secreted proteins, a function that is attributed to its ER- localized domain with a structure that bears a strong resemblance to another luminal ER chaperone and Ca-binding protein known as calreticulin. Studies have discovered that the cytosolic C-terminal domain of calnexin undergoes distinct post-translational modifications and interacts with a variety of proteins. Here, we discuss recent findings and hypothesize that the post-translational modifications of the calnexin C-terminal domain and its interaction with specific cytosolic proteins play a role in coordinating ER functions with events taking place in the cytosol and other cellular compartments.
钙连蛋白是一种Ⅰ型内质网（ER）整合膜蛋白，具有一个位于内质网腔的 N 端结构域和一个延伸到细胞质的 C 端结构域。钙连蛋白通常被称为一种分子伴侣，参与膜相关和分泌蛋白的折叠和质量控制，这一功能归因于其内质网定位结构域，其结构与另一种内质网腔伴侣和 Ca 结合蛋白——钙网蛋白具有很强的相似性。研究发现，钙连蛋白的细胞质 C 端结构域会发生不同的翻译后修饰，并与多种蛋白质相互作用。在这里，我们讨论了最近的发现，并假设钙连蛋白 C 端结构域的翻译后修饰及其与特定细胞质蛋白的相互作用在协调内质网功能与细胞质和其他细胞区室中的事件方面发挥作用。
