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

Yu, Lu-Gang, Andrews, Nigel, Weldon, Mike, Gerasimenko, Oleg Vsevolodovich, Campbell, Barry J., Singh, Ravinder, Grierson, Ian, Petersen, Ole Holger and Rhodes, Jonathan M. 2002. 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. Journal of Biological Chemistry 277 (27) , pp. 24538-24545. 10.1074/jbc.M203550200

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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-β1,3-N-acetylgalactosamine-α) and is shown to be essential for nuclear localization sequence-dependent nuclear protein import.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences Systems Immunity Research Institute (SIURI)
Publisher:	American Society for Biochemistry and Molecular Biology
ISSN:	0021-9258
Last Modified:	04 Jun 2017 06:38
URI:	http://orca.cf.ac.uk/id/eprint/63157

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