| First Author | Knoll M | Year | 2012 |
| Journal | J Immunol | Volume | 188 |
| Issue | 12 | Pages | 6010-7 |
| PubMed ID | 22566564 | Mgi Jnum | J:188886 |
| Mgi Id | MGI:5442493 | Doi | 10.4049/jimmunol.1200071 |
| Citation | Knoll M, et al. (2012) The non-Ig parts of the VpreB and lambda5 proteins of the surrogate light chain play opposite roles in the surface representation of the precursor B cell receptor. J Immunol 188(12):6010-7 |
| abstractText | The VpreB and lambda5 proteins, together with Igmu-H chains, form precursor BCRs (preBCRs). We established lambda5(-/-)/VpreB1(-/-)/VpreB2(-/-) Abelson virus-transformed cell lines and reconstituted these cells with lambda5 and VpreB in wild-type form or with a deleted non-Ig part. Whenever preBCRs had the non-Ig part of lambda5 deleted, surface deposition was increased, whereas deletion of VpreB non-Ig part decreased it. The levels of phosphorylation of Syk, SLP65, or PLC-gamma2, and of Ca(2+) mobilization from intracellular stores, stimulated by muH chain crosslinking Ab were dependent on the levels of surface-bound preBCRs. It appears that VpreB probes the fitness of newly generated VH domains of IgH chains for later pairing with IgL chains, and its non-Ig part fixes the preBCRs on the surface. By contrast, the non-Ig part of lambda5 crosslinks preBCRs for downregulation and stimulation. |
