Departments of Ophthalmology and Biochemistry, Ross Eye Institute, University at Buffalo, State University of New York, Buffalo, NY, USA.
SUNY Eye Institute, State University of New York, Buffalo, NY, USA.
Adv Exp Med Biol. 2018;1074:421-427. doi: 10.1007/978-3-319-75402-4_52.
The molecular chaperone endoplasmic reticulum protein 29 (ERp29) plays a critical role in protein folding, trafficking, and secretion. Though ubiquitously expressed, ERp29 is upregulated in response to ER stress and is found at higher levels in certain cell types such as secretory epithelial cells and neurons. As an ER resident protein, ERp29 shares many structural and functional similarities with protein disulfide isomerases, but is not regarded as part of this family due to several key differences. The broad expression and myriad roles of ERp29 coupled with its upregulation via the unfolded protein response (UPR) upon ER stress have implicated ERp29 in a range of cellular processes and diseases. We summarize the diverse activities of ERp29 in protein trafficking, cell survival and apoptosis, and ER homeostasis and highlight a potential role of ERp29 in neuroprotection in retinal and neurodegenerative diseases.
内质网蛋白 29(ERp29)是一种分子伴侣,在蛋白质折叠、运输和分泌过程中发挥着关键作用。虽然 ERp29 广泛表达,但它会响应内质网应激而上调,并在某些细胞类型(如分泌上皮细胞和神经元)中表达水平更高。作为内质网驻留蛋白,ERp29 在结构和功能上与蛋白质二硫键异构酶有许多相似之处,但由于几个关键差异,并不被认为是该家族的一部分。ERp29 的广泛表达和多种作用,以及其在内质网应激时通过未折叠蛋白反应(UPR)而上调,使其参与了多种细胞过程和疾病。我们总结了 ERp29 在蛋白质运输、细胞存活和凋亡、内质网稳态方面的多种活性,并强调了 ERp29 在视网膜和神经退行性疾病中的神经保护作用的潜力。