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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-β activation and cellular responses to B cell receptor (BCR) cross-linking in vitro. Introduction of a constitutively active IKK-β 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-β activation, thereby contributing to T cell-independent immune responses.


Kohei Kometani, Takayuki Yamada, Yoshiteru Sasaki, Tadashi Yokosuka, Takashi Saito, Klaus Rajewsky, Masamichi Ishiai, Masaki Hikida, Tomohiro Kurosaki. CIN85 drives B cell responses by linking BCR signals to the canonical NF-kappaB pathway. The Journal of experimental medicine. 2011 Jul 4;208(7):1447-57

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PMID: 21708930

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