| First Author | Ubelhart R | Year | 2010 |
| Journal | Nat Immunol | Volume | 11 |
| Issue | 8 | Pages | 759-65 |
| PubMed ID | 20622883 | Mgi Jnum | J:162389 |
| Mgi Id | MGI:4818821 | Doi | 10.1038/ni.1903 |
| Citation | Ubelhart R, et al. (2010) N-linked glycosylation selectively regulates autonomous precursor BCR function. Nat Immunol 11(8):759-65 |
| abstractText | Developing B cells express distinct classes of B cell antigen receptors (BCRs) that differ in their heavy chain (HC). Although only muHC is expressed in early stages, deltaHC-containing BCRs dominate on the surface of mature B cells. The reason for the tightly regulated expression of these receptors is poorly understood. Here we show that muHC was specifically required for precursor BCR (pre-BCR) function and that deltaHC was unable to form a functional pre-BCR. A conserved asparagine (N)-linked glycosylation site at position 46 (N46) in the first conserved domain of muHC was absolutely required for pre-BCR function, and swapping that domain with deltaHC resulted in a functional deltaHC-containing pre-BCR. When tested in the context of the BCR, muHC with a mutant N46 showed normal function, which indicated that N46-glycosylation is specifically required for pre-BCR function. Our results suggest an unexpected mode of pre-BCR function, in which binding of the surrogate light chain to N46 mediates autonomous crosslinking and, concomitantly, receptor formation. |
