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

Nature volume 356, pages 246–248 (1992)Cite this article

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-α and Ig-β1–8. The Ig-α and Ig-β proteins form a disulphide-linked α/β heterodimer and are encoded by the mb-l (refs 9, 10) and B29 genes11,12, respectively13,14. Surface expression of the membrane-bound IgM molecule requires assembly with the α/βheterodimer1,3,4,8. The IgD molecule, however, can be expressed on the cell surface in an α/β-dependent and -independent form8,15. We show here that in the α/β -independent form the IgD molecule is anchored in the plasma membrane through a glycosyl-phos-phatidylinositol linker. In the presence of the α/β heterodimer, most of the otherwise glycosyl-phosphatidylinositol-linked IgD molecule is expressed on the cell surface as transmembrane proteins.

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Authors and Affiliations

  1. Max-Planck Institut für Immunbiologie, Stübeweg 51, D-7800, Freiburg, Germany

    Jürgen Wienands & Michael Reth

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  1. Jürgen Wienands
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  2. Michael Reth
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Wienands, J., Reth, M. Glycosyl-phosphatidylinositol linkage as a mechanism for cell-surface expression of immunoglobulin D. Nature 356, 246–248 (1992). https://doi.org/10.1038/356246a0

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