Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking Academic Article uri icon

Overview

MeSH Major

  • Carrier Proteins
  • Caveolins
  • Cell Membrane
  • Glycosylphosphatidylinositols
  • Receptors, Cell Surface

abstract

  • Glycosyl-phosphatidylinositol (GPI)-anchored proteins have been reported to reside in clusters collected over small membrane invaginations called caveolae. The detection of different GPI-anchored proteins with fluorescently labeled monoclonal antibodies showed that these proteins are not constitutively concentrated in caveolae; they enter these structures independently after cross-linking with polyclonal secondary antibodies. Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms these observations. Thus, multimerization of GPI-anchored proteins regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.

publication date

  • June 24, 1994

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 7516582

Additional Document Info

start page

  • 1948

end page

  • 51

volume

  • 264

number

  • 5167