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Mol Immunol. 2010 Jan;47(4):878-82. doi: 10.1016/j.molimm.2009.10.016. Epub 2009 Nov 27.

Requirement of the cytoplasmic portion for dimer formation of Fcalpha/micro receptor expressed on cell surface.

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Department of Immunology, Institute of Basic Medical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba, 1-1-1 Ten-nohdai, Tsukuba, Ibaraki 305-8575, Japan.


Fcalpha/mu receptor (Fcalpha/muR), an Fc receptor for IgA and IgM, is the only Fc receptor for IgM identified on hematopoietic cells in human and rodents and for IgA in rodents. Fcalpha/microR is a type 1 transmembrane protein containing one immunoglobulin-like domain in the extracellular portion. Both human and mouse Fcalpha/microR mediate endocytosis of the ligands IgA and IgM, for which the cytoplasmic portion of Fcalpha/microR is responsible. However, molecular characteristics of Fcalpha/muR involved in the function have been incompletely understood. Here, we show that both monomeric and dimeric Fcalpha/microR are expressed in a mouse B cell line BCL1-B20 and BW5147 or Ba/F3 transfectants stably expressing Fcalpha/microR. We also show that the dimeric, but not monomeric, Fcalpha/microR is preferentially localized to the cell surface of the transfectants. BW5147 transfectant expressing mutant Fcalpha/microR lacking the cytoplasmic portion expressed only the monomeric Fcalpha/microR. These results suggest that the cytoplasmic portion is required for the dimer formation and thus for efficient cell surface expression of Fcalpha/microR.

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