Kato Koichi, Kamiya Yukiko
Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
Glycobiology. 2007 Oct;17(10):1031-44. doi: 10.1093/glycob/cwm046. Epub 2007 Apr 20.
Processing of the N-glycans is coupled with the fates of glycoproteins in cells. A series of processing intermediates of high-mannose-type glycans are generated by specific glycosidases and thereby express biological signals recognized by intracellular lectins operating as molecular chaperones, cargo receptors, and ubiquitin ligases. Consequently, these lectins govern the intracellular processes of folding, transport, and degradation of the carrier polypeptides. To understand the underlying mechanisms of glycoprotein-fate determination, structural information on modes of molecular recognition by these lectins and enzymes is undoubtedly important. This article overviews our current knowledge of the structural basis for quality control of glycoproteins in cells.
N-聚糖的加工与细胞中糖蛋白的命运相关联。一系列高甘露糖型聚糖的加工中间体由特定糖苷酶产生，从而表达作为分子伴侣、货物受体和泛素连接酶发挥作用的细胞内凝集素所识别的生物信号。因此，这些凝集素控制着载体多肽的细胞内折叠、运输和降解过程。为了理解糖蛋白命运决定的潜在机制，这些凝集素和酶的分子识别模式的结构信息无疑很重要。本文概述了我们目前对细胞中糖蛋白质量控制结构基础的认识。
