Abstract
N-linked oligosaccharides attached to proteins act as tags for glycoprotein quality control, ensuring their appropriate folding and trafficking in cells. Interactions with a variety of intracellular lectins determine glycoprotein fates. Monoglucosylated glycoforms are the hallmarks of incompletely folded glycoproteins in the protein quality-control system, in which glucosidase II and UDP-glucose/glycoprotein glucosyltransferase are, respectively, responsible for glucose trimming and attachment. In this review, we summarize a recently emerging view of the structural basis of the functional mechanisms of these key enzymes as well as substrate N-linked oligosaccharides exhibiting flexible structures, as revealed by applying a series of biophysical techniques including small-angle X-ray scattering, X-ray crystallography, high-speed atomic force microscopy , electron microscopy , and computational simulation in conjunction with NMR spectroscopy.
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Acknowledgments
This work was supported in part by the Okazaki ORION project and Grants-in-Aid for Scientific Research (Grant Numbers JP25121730 to T.S., and JP25102008, JP24249002 to K.K.) from the Ministry of Education, Culture, Sports, Science and Technology, Japan, the PRESTO project (Grant Number JPMJPR13L5 to T.S.) from the Japan Science and Technology Agency, and by Grant-in-Aid for Research in Nagoya City University.
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Satoh, T., Kato, K. (2018). Structural Aspects of ER Glycoprotein Quality-Control System Mediated by Glucose Tagging. In: Yamaguchi, Y., Kato, K. (eds) Glycobiophysics. Advances in Experimental Medicine and Biology, vol 1104. Springer, Singapore. https://doi.org/10.1007/978-981-13-2158-0_8
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