Similar processes mediate glycopeptide export from the endoplasmic reticulum in mammalian cells and Saccharomyces cerevisiae

Proceedings of the National Academy of Sciences of the United States of America
Karin Römisch, B R Ali

Abstract

Glycopeptides are transported from the lumen of the yeast endoplasmic reticulum (ER) to the cytosol and in contrast to secretory proteins do not enter ER-to-Golgi transport vesicles. In a cell-free system, this process is ATP- and cytosol-dependent. While yeast cytosol promotes the export of glycopeptides from mammalian ER in vitro, glycopeptide release cannot be detected in the presence of mammalian cytosol. We demonstrate that this is due to an N-glycanase activity in mammalian cytosol rather than lack of glycopeptide transport activity in mammalian microsomes. Monitoring the amount of glycopeptide enclosed in ER membranes we show the cytosol- and ATP-dependent release of glycopeptide from mammalian microsomes. The fact that glycopeptide export can be achieved with ER and cytosol derived from heterologous sources indicates that glycopeptide export from the ER is an important process conserved during evolution.

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Citations

Apr 12, 2000·Proceedings of the National Academy of Sciences of the United States of America·P GilleceK Römisch
Jun 1, 2000·The Journal of Cell Biology·T SuzukiW J Lennarz
Jan 20, 2005·Journal of Biochemical and Biophysical Methods·Bassam R S AliMark C Field
Dec 6, 2014·Seminars in Cell & Developmental Biology·Hiroto HirayamaTadashi Suzuki
Oct 11, 2005·Annual Review of Cell and Developmental Biology·Karin Römisch
May 30, 1998·The Journal of Biological Chemistry·T SuzukiW J Lennarz
Jul 27, 2000·The Journal of Biological Chemistry·B R AliM C Field
Jul 31, 1999·The Journal of Biological Chemistry·J B Hwang, S C Frost
Apr 30, 2002·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Tadashi SuzukiWilliam J Lennarz
Oct 8, 1999·Trends in Cell Biology·S E Moore

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