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.

有限的蛋白水解过程是影响分泌蛋白的必不可少且普遍存在的翻译后修饰（PTM）；无法调节过程通常与疾病有关。糖基化也是一种普遍存在的蛋白PTM，在蛋白水解位点附近的位点特异性O-糖基化可以调节和指导原蛋白转化酶，整联蛋白和金属蛋白酶（ADAM）的活性，以及​​影响许多类别蛋白的激活或失活的金属蛋白酶的活性。蛋白，包括G蛋白偶联受体（GPCR）。在这里，我们总结了新兴数据，这些数据表明O-糖基化是有限蛋白水解的关键调节剂，并强调了多个PTM之间发生串扰的可能性。