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• W2120996859 abstract "Some secretory proteins leave the endoplasmic reticulum (ER) by a receptor-mediated cargo capture mechanism, but the signals required for the cargo-receptor interaction are largely unknown. Here, we describe a novel targeting motif that is composed of a high-mannose type oligosaccharide intimately associated with a surface-exposed peptide β-hairpin loop. The motif accounts for lectin ERGIC-53–assisted ER-export of the lyososomal enzyme procathepsin Z. The second oligosaccharide chain of procathepsin Z exhibits no binding activity for ERGIC-53, illustrating the selective lectin properties of ERGIC-53. Our data suggest that the conformation-based motif is only present in fully folded procathepsin Z and that its recognition by ERGIC-53 reflects a quality control mechanism that acts complementary to the primary folding machinery in the ER. A similar oligosaccharide/β-hairpin loop structure is present in cathepsin C, another cargo of ERGIC-53, suggesting the general nature of this ER-exit signal. To our knowledge this is the first documentation of an ER-exit signal in soluble cargo in conjunction with its decoding by a transport receptor." @default.
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• W2120996859 date "2005-03-01" @default.
• W2120996859 modified "2023-10-18" @default.
• W2120996859 title "Carbohydrate- and Conformation-dependent Cargo Capture for ER-Exit" @default.
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• W2120996859 doi "https://doi.org/10.1091/mbc.e04-08-0708" @default.
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