Molecular characterization of the dimer formation of Fcα/μ receptor (CD351)
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,...
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| Veröffentlicht in: | Molecular immunology 2013-11, Vol.56 (1-2), p.23-27 |
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| container_title | Molecular immunology |
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| creator | Takagaki, Kana Satoh, Kazuki Honda, Shin-ichiro Shibuya, Akira |
| description | 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. |
| doi_str_mv | 10.1016/j.molimm.2013.04.003 |
| format | Article |
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Instead, our data suggest that Fcα/μR forms heterodimers with an as-yet-unknown molecule with a molecular weight of 60–70kDa.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cell Line, Tumor</subject><subject>Dimer formation</subject><subject>Fc receptor</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>IgA</subject><subject>IgM</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Receptors, Fc - chemistry</subject><subject>Receptors, Fc - genetics</subject><subject>Receptors, Fc - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transfection</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1OGzEUha2qqKRp3wChWaaLGa5_49kgVSm0SCA2sLY89h3F0Uwc7AkSvBV7noFn6kShWZbVla6-c470EXJCoaJA1dmq6mMX-r5iQHkFogLgn8iE6jkrayrYZzIZMVpKXcMx-ZrzCgAUKPmFHDOulOQaJuTmJnbotp1NhVvaZN2AKTzbIcR1EdtiWGLhQ4-paGPqD-9L9_Zy9vZaJHS4GWIqZotfXNIf38hRa7uM39_vlNxfXtwt_pTXt7-vFj-vSye0HErdMjbXFGpwHig01jdUtEwjl-ClbVirPYBXNZMKlfBUCEBsGgrQ0tpqPiWzfe8mxYct5sH0ITvsOrvGuM2GSjVKmTPBP0b5OMOlYDtU7FGXYs4JW7NJobfpyVAwO-dmZfbOzc65AWFG52Ps9H1h2_ToD6F_kkfgfA_gqOQxYDLZBVw79GEUOBgfw_8X_gIZcpOT</recordid><startdate>201311</startdate><enddate>201311</enddate><creator>Takagaki, Kana</creator><creator>Satoh, Kazuki</creator><creator>Honda, Shin-ichiro</creator><creator>Shibuya, Akira</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>201311</creationdate><title>Molecular characterization of the dimer formation of Fcα/μ receptor (CD351)</title><author>Takagaki, Kana ; Satoh, Kazuki ; Honda, Shin-ichiro ; Shibuya, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c485t-8f22781090cd010badb14f28e350d5ab2f8d00d69256e64d1440eebb100f19a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cell Line, Tumor</topic><topic>Dimer formation</topic><topic>Fc receptor</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>IgA</topic><topic>IgM</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Receptors, Fc - chemistry</topic><topic>Receptors, Fc - genetics</topic><topic>Receptors, Fc - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takagaki, Kana</creatorcontrib><creatorcontrib>Satoh, Kazuki</creatorcontrib><creatorcontrib>Honda, Shin-ichiro</creatorcontrib><creatorcontrib>Shibuya, Akira</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takagaki, Kana</au><au>Satoh, Kazuki</au><au>Honda, Shin-ichiro</au><au>Shibuya, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of the dimer formation of Fcα/μ receptor (CD351)</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>2013-11</date><risdate>2013</risdate><volume>56</volume><issue>1-2</issue><spage>23</spage><epage>27</epage><pages>23-27</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><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. 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| ispartof | Molecular immunology, 2013-11, Vol.56 (1-2), p.23-27 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Blotting, Western Cell Line, Tumor Dimer formation Fc receptor Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism IgA IgM Mice Molecular Sequence Data Mutation Protein Binding Protein Multimerization Receptors, Fc - chemistry Receptors, Fc - genetics Receptors, Fc - metabolism Sequence Homology, Amino Acid Transfection |
| title | Molecular characterization of the dimer formation of Fcα/μ receptor (CD351) |
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