Sorting of GPI-anchored Proteins to Glycolipid-Enriched Membrane Subdomains During Transport to the Apical Cell Surface

Cell. 1992 Feb 7;68(3):533-44. doi: 10.1016/0092-8674(92)90189-j.

Abstract

We show that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form. Under these conditions, the protein is associated with detergent-resistant sheets and vesicles that contain other GPI-anchored proteins and are enriched in glycosphingolipids, but do not contain a basolateral marker protein. The protein is recovered in this complex only after it has been transported to the Golgi complex, suggesting that protein-sphingolipid microdomains form in the Golgi apparatus and plasma membrane and supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acid Phosphatase / analysis*
  • Animals
  • Cell Compartmentation
  • Cell Line
  • Cell Membrane / chemistry*
  • Dogs
  • Glycolipids / analysis*
  • Glycosylphosphatidylinositols
  • Golgi Apparatus / chemistry*
  • Liposomes / chemistry
  • Membrane Lipids / analysis
  • Membrane Proteins / analysis
  • Phosphatidylinositols / analysis*

Substances

  • Glycolipids
  • Glycosylphosphatidylinositols
  • Liposomes
  • Membrane Lipids
  • Membrane Proteins
  • Phosphatidylinositols
  • Acid Phosphatase