| First Author | Ni CY | Year | 2008 |
| Journal | J Immunol | Volume | 180 |
| Issue | 11 | Pages | 7107-11 |
| PubMed ID | 18490708 | Mgi Jnum | J:136353 |
| Mgi Id | MGI:3796022 | Doi | 10.4049/jimmunol.180.11.7107 |
| Citation | Ni CY, et al. (2008) Cutting edge: K63-linked polyubiquitination of NEMO modulates TLR signaling and inflammation in vivo. J Immunol 180(11):7107-11 |
| abstractText | Transcription factor NF-kappaB controls the expression of multiple genes involved in immunity and inflammation. The initial activation and duration of NF-kappaB signaling is regulated by posttranslational modifications to IkappaB kinase, which earmarks inhibitors of NF-kappaB for degradation. Prior studies suggest that K63-linked ubiquitination of NEMO (NF-kappaB essential modulator), an IkappaB kinase regulatory subunit, is critical for NF-kappaB and MAPK signaling following engagement of Ag receptors. We now demonstrate that NF-kappaB and MAPK pathways are largely unaffected in primary cells from mice harboring a ubiquitination-defective form of NEMO, NEMO-KR. TLR- but not Ag receptor-induced cellular responses are impaired in NEMO-KR mice, which are more resistant to LPS-induced endotoxic shock than wild-type animals. Thus, one function of NEMO ubiquitination is to fine tune innate immune responses under TLR control. |
