GD3 glycosphingolipid contributes to Fas-mediated apoptosis via association with ezrin cytoskeletal protein

FEBS Lett. 2001 Sep 28;506(1):45-50. doi: 10.1016/s0014-5793(01)02776-4.

Abstract

Efficiency of Fas-mediated apoptosis of lymphoid cells is regulated, among other means, by a mechanism involving its association with ezrin, a cytoskeletal protein belonging to the 4.1 family of proteins. In the present work, we provide evidence for a further molecule that associates to ezrin in Fas-triggered apoptosis, the disialoganglioside GD3. In fact, as an early event, GD3 redistributed in membrane-associated domains in uropods and co-localized with ezrin. Co-immunoprecipitation analyses confirmed this result, indicating a GD3-ezrin association. Altogether, these results are suggestive for a role of GD3 in Fas/ezrin-mediated apoptosis, supporting the view that uropods contain a multimolecular signaling complex involved in Fas-mediated apoptosis.

MeSH terms

  • Apoptosis / physiology*
  • Cell Line
  • Chromatography, Thin Layer
  • Cytoskeletal Proteins
  • Gangliosides / metabolism
  • Gangliosides / physiology*
  • Humans
  • Microscopy, Confocal
  • Microscopy, Electron, Scanning
  • Microscopy, Fluorescence
  • Phosphoproteins / metabolism*
  • Precipitin Tests
  • fas Receptor / physiology*

Substances

  • Cytoskeletal Proteins
  • Gangliosides
  • Phosphoproteins
  • ezrin
  • fas Receptor
  • ganglioside, GD3