Molecular characterization of the dimer formation of Fcα/μ receptor (CD351)
Molecular characterization of the dimer formation of Fcα/μ receptor (CD351)
复制标题
Fcα/μ 受体 (CD351) 二聚体形成的分子表征
DOI:
10.1016/j.molimm.2013.04.003
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发表时间:
2013
期刊:
影响因子:
3.6
通讯作者:
Shibuya A
中科院分区:
文献类型:
--
作者:
Takagaki K;Satoh K;Honda S;Shibuya A
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 60–70kDa.