Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark.
Trends Biochem Sci. 2018 Apr;43(4):269-284. doi: 10.1016/j.tibs.2018.02.005. Epub 2018 Mar 2.
Limited proteolytic processing is an essential and ubiquitous post-translational modification (PTM) affecting secreted proteins; failure to regulate the process is often associated with disease. Glycosylation is also a ubiquitous protein PTM and site-specific O-glycosylation in close proximity to sites of proteolysis can regulate and direct the activity of proprotein convertases, a disintegrin and metalloproteinases (ADAMs), and metalloproteinases affecting the activation or inactivation of many classes of proteins, including G-protein-coupled receptors (GPCRs). Here, we summarize the emerging data that suggest O-glycosylation to be a key regulator of limited proteolysis, and highlight the potential for crosstalk between multiple PTMs.
有限的蛋白水解加工是一种影响分泌蛋白的基本且普遍存在的翻译后修饰（PTM）；该过程的调节失败通常与疾病有关。糖基化也是一种普遍存在的蛋白质 PTM，靠近蛋白水解位点的特定 O-糖基化可以调节和指导前蛋白转化酶、去整合素和金属蛋白酶（ADAMs）以及金属蛋白酶的活性，这些酶会影响许多类蛋白质（包括 G 蛋白偶联受体（GPCRs））的激活或失活。在这里，我们总结了一些新出现的数据，表明 O-糖基化是有限蛋白水解的关键调节因子，并强调了多种 PTM 之间相互作用的潜力。
