Abstract
Protein sorting in the secretory pathway is an essential step to route proteins to their proper locations. A number of secretory proteins contain intrinsic sorting signals that are recognized by transport machineries. Efficient sorting of several secretory proteins requires cargo receptors that recognize the sorting signals of specific proteins and sort them into transport vesicles. In the early secretory pathway from the endoplasmic reticulum (ER), the cargo receptors function as linkers between the secretory proteins and coat protein complex II (COPII). Most secretory proteins are posttranslationally modified by the addition of sugar chains in the ER. Several lines of evidence indicate that these glycan structures act as signals for transport of the modified proteins and determine their final destinations. In the secretory pathway, there are several lectin-type cargo receptors that recognize specific glycan structures on proteins. The interactions between glycoproteins and cargo receptors are dependent upon the environment, such as the pH in organelles, as well as the glycan structures. Impairment of cargo receptors causes several diseases through inefficient delivery of their target molecules. In this review, we describe the current understanding of the sorting and transport mechanisms of glycoproteins from the ER in mammalian cells.
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Fujita, M., Gao, XD., Kinoshita, T. (2015). Glycan-Mediated Protein Transport from the Endoplasmic Reticulum. In: Suzuki, T., Ohtsubo, K., Taniguchi, N. (eds) Sugar Chains. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55381-6_2
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