| First Author | Kläsener K | Year | 2014 |
| Journal | Elife | Volume | 3 |
| Pages | e02069 | PubMed ID | 24963139 |
| Mgi Jnum | J:220497 | Mgi Id | MGI:5634874 |
| Doi | 10.7554/eLife.02069.001 | Citation | Klasener K, et al. (2014) B cell activation involves nanoscale receptor reorganizations and inside-out signaling by Syk. Elife 3:e02069 |
| abstractText | Binding of antigen to the B cell antigen receptor (BCR) initiates a multitude of events resulting in B cell activation. How the BCR becomes signaling-competent upon antigen binding is still a matter of controversy. Using a high-resolution proximity ligation assay (PLA) to monitor the conformation of the BCR and its interactions with co-receptors at a 10-20 nm resolution, we provide direct evidence for the opening of BCR dimers during B cell activation. We also show that upon binding Syk opens the receptor by an inside-out signaling mechanism that amplifies BCR signaling. Furthermore, we found that on resting B cells, the coreceptor CD19 is in close proximity with the IgD-BCR and on activated B cells with the IgM-BCR, indicating nanoscale reorganization of receptor clusters during B cell activation.DOI: http://dx.doi.org/10.7554/eLife.02069.001. |
