Concentration of GPI-anchored proteins upon ER exit in yeast.
- Castillon GA Department of Biochemistry, University of Geneva, Sciences II, 30 quai Ernest Ansermet, CH-1211 Geneva, Switzerland.
- Watanabe R
- Taylor M
- Schwabe TM
- Riezman H
- 2008-12-05
Published in:
- Traffic (Copenhagen, Denmark). - 2009
Amino Acid Transport Systems
Cell Wall
Cytoplasmic Vesicles
Endoplasmic Reticulum
Glucose Transport Proteins, Facilitative
Glycosylphosphatidylinositols
Membrane Glycoproteins
Membrane Proteins
Monosaccharide Transport Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Temperature
Vesicular Transport Proteins
English
Previous biochemical work has revealed two parallel routes of exit from the endoplasmic reticulum (ER) in the yeast Saccharomyces cerevisiae, one seemingly specific for glycosyl-phosphatidylinositol (GPI)-anchored proteins. Using the coat protein II (COPII) mutant sec31-1, we visualized ER exit sites (ERES) and identified three distinct ERES populations in vivo. One contains glycosylated pro-alpha-factor, the second contains the GPI-anchored proteins Cwp2p, Ccw14p and Tos6p and the third is enriched with the hexose transporter, Hxt1p. Concentration of GPI-anchored proteins prior to budding requires anchor remodeling, and Hxt1p incorporation into ERES requires the COPII components Sec12p and Sec16p. Additionally, we have found that GPI-anchored protein ER exit is controlled by the p24 family member Emp24p, whereas ER export of most transmembrane proteins requires the Cornichon homologue Erv14p.
- Language
-
- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1111/j.1600-0854.2008.00857.x
- PMID 19054390
- Persistent URL
- https://sonar.ch/global/documents/205778
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