| First Author | Kometani K | Year | 2011 |
| Journal | J Exp Med | Volume | 208 |
| Issue | 7 | Pages | 1447-57 |
| PubMed ID | 21708930 | Mgi Jnum | J:176805 |
| Mgi Id | MGI:5292774 | Doi | 10.1084/jem.20102665 |
| Citation | Kometani K, et al. (2011) CIN85 drives B cell responses by linking BCR signals to the canonical NF-kappaB pathway. J Exp Med 208(7):1447-57 |
| abstractText | CIN85, an adaptor protein which binds the C-terminal domain of tyrosine phosphorylated Cbl and Cbl-b, has been thought to be involved in the internalization and subsequent degradation of receptors. However, its physiological function remains unclear. To determine its role in B cells, we used Mb1-cre to generate mice with a B cell-specific deletion of CIN85. These mice had impaired T cell-independent type II antibody responses in vivo and diminished IKK-beta activation and cellular responses to B cell receptor (BCR) cross-linking in vitro. Introduction of a constitutively active IKK-beta construct corrected the defective antibody responses as well as cellular responses in the mutant mice. Together, our results suggest that CIN85 links the BCR to IKK-beta activation, thereby contributing to T cell-independent immune responses. |
