Glycosyl-phosphatidylinositol linkage as a mechanism for cell-surface expression of immunoglobulin D

Nature. 1992 Mar 19;356(6366):246-8. doi: 10.1038/356246a0.

Abstract

The B-cell antigen receptor of the IgM and IgD class is a multimeric complex consisting of the membrane-bound form of the immunoglobulin molecule and two other proteins, Ig-alpha and Ig-beta. The Ig-alpha and Ig-beta proteins form a disulphide-linked alpha/beta heterodimer and are encoded by the mb-1 (ref 9, 10) and B29 genes, respectively. Surface expression of the membrane-bound IgM molecule requires assembly with the alpha/beta heterodimer. The IgD molecule, however, can be expressed on the cell surface in an alpha/beta-dependent and -independent form. We show here that in the alpha/beta-independent form the IgD molecule is anchored in the plasma membrane through a glycosyl-phosphatidylinositol linker. In the presence of the alpha/beta heterodimer, most of the otherwise glycosyl-phosphatidylinositol-linked IgD molecule is expressed on the cell surface as transmembrane proteins.

MeSH terms

  • Biological Transport
  • Blotting, Western
  • Cell Line
  • Cell Membrane / immunology*
  • Cloning, Molecular
  • Gene Expression*
  • Glycolipids / metabolism*
  • Glycosylphosphatidylinositols
  • Immunoglobulin D / analysis
  • Immunoglobulin D / genetics*
  • Immunoglobulin D / metabolism
  • Macromolecular Substances
  • Multiple Myeloma / immunology
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphatidylinositols / metabolism*
  • Phosphoric Diester Hydrolases / metabolism
  • Transfection

Substances

  • Glycolipids
  • Glycosylphosphatidylinositols
  • Immunoglobulin D
  • Macromolecular Substances
  • Phosphatidylinositols
  • Phosphoric Diester Hydrolases
  • Phosphatidylinositol Diacylglycerol-Lyase