| First Author | Tolar P | Year | 2005 |
| Journal | Nat Immunol | Volume | 6 |
| Issue | 11 | Pages | 1168-76 |
| PubMed ID | 16200067 | Mgi Jnum | J:112561 |
| Mgi Id | MGI:3662782 | Doi | 10.1038/ni1262 |
| Citation | Tolar P, et al. (2005) The initiation of antigen-induced B cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer. Nat Immunol 6(11):1168-76 |
| abstractText | Binding of antigen to the B cell antigen receptor (BCR) triggers signaling that ultimately leads to B cell activation. Using quantitative fluorescence resonance energy transfer imaging, we provide evidence here that the BCR is a monomer on the surface of resting cells. Binding of multivalent antigen clustered the BCR, resulting in the simultaneous phosphorylation of and a conformational change in the BCR cytoplasmic domains from a closed to an open form. Notably, the open conformation required immunoreceptor tyrosine-activation motif and continuous Src family kinase activity but not binding of the kinase Syk. Thus, the initiation of BCR signaling is a very dynamic process accompanied by reversible conformational changes induced by Src family kinase activity. |
