| RRC ID |
38265
|
| Author |
Cho Y, Honda S, Yoshizawa Y, Takagaki K, Usui K, Shibuya A.
|
| Title |
Requirement of the cytoplasmic portion for dimer formation of Fcalpha/micro receptor expressed on cell surface.
|
| Journal |
Mol Immunol
|
| Abstract |
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.
|
| Volume |
47(4)
|
| Pages |
878-82
|
| Published |
2010-1-1
|
| DOI |
10.1016/j.molimm.2009.10.016
|
| PII |
S0161-5890(09)00788-3
|
| PMID |
19945166
|
| MeSH |
Animals
Cell Membrane / metabolism*
Cytoplasm / metabolism*
Humans
Ligands
Mice
Mutant Proteins / chemistry
Mutant Proteins / metabolism
Protein Multimerization*
Receptors, Fc / chemistry*
Receptors, Fc / metabolism*
Structure-Activity Relationship
Transfection
|
| IF |
3.641
|
| Times Cited |
6
|
|
WOS Category
|
IMMUNOLOGY
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Human and Animal Cells |
|
