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|Title:||Mutations which abolish phosphorylation of the TRAF-binding domain of TNF receptor 2 enhance receptor-mediated NF-κB activation|
|Authors:||Ng, P.W.P. |
|Citation:||Ng, P.W.P., Jänicke, R.U., Porter, A.G. (1998-03-27). Mutations which abolish phosphorylation of the TRAF-binding domain of TNF receptor 2 enhance receptor-mediated NF-κB activation. Biochemical and Biophysical Research Communications 244 (3) : 756-762. ScholarBank@NUS Repository. https://doi.org/10.1006/bbrc.1998.8323|
|Abstract:||We demonstrate that a 41 amino acid region (amino acids 379 to 419) in the cytoplasmic domain of tumor necrosis factor receptor 2 (TNFR2) is phosphorylated by unidentified kinase(s) both in vitro and in vivo. This domain (denoted x1c) corresponds almost exactly to the previously identified TRAF-binding domain and is by itself sufficient as a substrate for phosphorylation. In addition, the x1c domain is also crucial for TNFR2-mediated NF-κB activation. The cytoplasmic domain of TNFR2 lacks tyrosines, and conversion of all 12 potential serine and threonine phosphorylation targets in x1c to alanines either had no effect on NF-κB activation or resulted in enhanced NF-κB activity, depending on the structural context of x1c. The results show that while the TRAF-binding domain of TNFR2 is a major target of kinases, its phosphorylation is not required for NF-κB activation. Our data moreover suggest that phosphorylation of x1c negatively regulates the activation of NF-κB.|
|Source Title:||Biochemical and Biophysical Research Communications|
|Appears in Collections:||Staff Publications|
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