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Mol Immunol. 2013 Nov;56(1-2):23-7. doi: 10.1016/j.molimm.2013.04.003. Epub 2013 May 9.

Molecular characterization of the dimer formation of Fcα/μ receptor (CD351).

Author information

1
Department of Immunology, Institute of Basic Medical Sciences, Faculty of Medicine, University of Tsukuba, Tsukuba, Ibaraki, Japan.

Abstract

Fcα/μR (CD351) is an Fc receptor for both IgA and IgM and forms an atypical dimer that is resistant to reduction by 2-mercaptoethanol or boiling. We previously demonstrated that the cytoplasmic portion of Fcα/μR is required for dimer formation and for its efficient cell-surface expression. However, the biochemical nature of these phenomena has not been determined. By using a BW5147 mouse cell line expressing deletion mutants of the cytoplasmic region of Fcα/μR, we found that the region spanning amino acids 504-523 was required for efficient cell-surface expression, whereas the region spanning amino acids 481-490 was required for dimmer formation. Immunoblotting analyses of transfectants simultaneously expressing Flag-tagged Fcα/μR and hemagglutinin-tagged Fcα/μR suggested that Fcα/μR does not form homodimers. Instead, our data suggest that Fcα/μR forms heterodimers with an as-yet-unknown molecule with a molecular weight of 60-70 kDa.

PMID:
23665380
DOI:
10.1016/j.molimm.2013.04.003
[Indexed for MEDLINE]

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