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Concentration of GPI-anchored proteins upon ER exit in yeast.

Traffic. 2009 Feb;10(2):186-200. Epub 2008 Nov 20
Guillaume A Castillon 1 , Reika Watanabe , Marcia Taylor , Tatjana M E Schwabe , Howard Riezman
Guillaume A Castillon 1 , Reika Watanabe , Marcia Taylor , Tatjana M E Schwabe , Howard Riezman

[No authors listed]

Author information
  • 1 Department of Biochemistry, University of Geneva, Sciences II, 30 quai Ernest Ansermet, CH-1211 Geneva, Switzerland.

摘要


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.