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ß₂-microglobulin is important for cell surface expression and pH-dependent IgG binding of human FcRn

Institute of Molecular and Cell Biology, Epithelial Cell Biology Laboratory, 30 Medical Drive, Singapore 117609, Republic of Singapore

^* Author for correspondence (e-mail: hunziker{at}imcb.nus.edu.sg )

Accepted 19 March 2002

FcRn is a heterodimer of an -chain and ß₂-microglobulin (ß₂m) and differs from other IgG Fc receptors in that it is structurally related to MHC class I molecules. Several functions attributed to FcRn are affected in ß₂-microglobulin (ß₂m)-deficient mice, suggesting that the -chain needs to assemble with ß₂m to form a functional receptor. However, the precise role of ß₂m in FcRn function is not known. Here we expressed the human FcRn -chain alone or in combination with ß₂m in human melanoma FO-1 cells. We show that ß₂m is important for cell surface expression of FcRn and that, in the absence of ß₂m, the receptor is retained in the endoplasmic reticulum. Furthermore, in the absence of ß₂m, IgG binding is decreased compared with that of native FcRn. Thus, assembly of the FcRn -chain with ß₂m is important for both transport of FcRn from the ER to the cell surface and efficient pH-dependent IgG binding.

Key words: Human immunoglobulin G, Major histocompatibility complex, Endoplasmic reticulum, Oligomerization

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