Glycotripeptides are released by yeast but not by mammalian microsomes
- 28 November 1994
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 355 (2) , 147-150
- https://doi.org/10.1016/0014-5793(94)01167-2
Abstract
Glycotripeptides generated in vivo in the endoplasmic reticulum (ER) have been used as markers to assess the rate of vesicular bulk flow from the ER via the Golgi apparatus to the plasma membrane in mammalian cells. The applicability of such glycotripeptides as markers for bulk flow along this pathway has been questioned by a report on non-vesicular release of glycotripeptides from yeast semi-intact spheroplasts. We have therefore investigated direct release of glycotripeptides from yeast and from mammalian microsomes and report here that such release is specific to the yeast system and cannot be detected in mammalian microsomes.Keywords
This publication has 12 references indexed in Scilit:
- Complete Golgi passage of glycotripeptides generated in the endoplasmic reticulum of mammalian cellsFEBS Letters, 1994
- Peptide Translocation by Variants of the Transporter Associated with Antigen ProcessingScience, 1993
- Distinct processes mediate glycoprotein and glycopeptide export from the endoplasmic reticulum in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences, 1992
- The rate of bulk flow from the Golgi to the plasma membraneCell, 1990
- Control of Protein Exit from the Endoplasmic ReticulumAnnual Review of Cell Biology, 1989
- Reconstitution of SEC gene product-dependent intercompartmental protein transportCell, 1988
- The rate of bulk flow from the endoplasmic reticulum to the cell surfaceCell, 1987
- BIOSYNTHETIC PROTEIN TRANSPORT AND SORTING BY THE ENDOPLASMIC RETICULUM AND GOLGIAnnual Review of Biochemistry, 1987
- Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis.The Journal of cell biology, 1986
- Xenopus oocytes can secrete bacterial β-lactamaseNature, 1984