An N-terminal truncated form of Orp150 is a cytoplasmic ligand for the anti-proliferative mushroom Agaricus bisporus lectin and is required for nuclear localization sequence-dependent nuclear protein import |
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Authors: | Yu Lu-Gang Andrews Nigel Weldon Mike Gerasimenko Oleg V Campbell Barry J Singh Ravinder Grierson Ian Petersen Ole H Rhodes Jonathan M |
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Affiliation: | Department of Medicine, The Henry Wellcome Laboratory of Molecular and Cellular Gastroenterology, University of Liverpool, Liverpool L69, United Kingdom. |
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Abstract: | Nuclear localization sequence-dependent nuclear protein import is essential for maintaining cell function and can be selectively blocked in epithelial cells by mushroom (Agaricus bisporus) lectin. Here we report that a major intracellular ligand for this lectin is an N-terminally truncated form of oxygen-regulated protein 150 (Orp150), which lacks the endoplasmic reticulum translocation signal peptide of full-length Orp150. This cytoplasmic form of Orp150 expresses the lectin carbohydrate ligand (sialyl-2,3-galactosyl-beta1,3-N-acetylgalactosamine-alpha) and is shown to be essential for nuclear localization sequence-dependent nuclear protein import. |
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