Role of Unphosphorylated, Newly Synthesized I (cid:107) B (cid:98) in Persistent Activation of NF- (cid:107) B
Role of Unphosphorylated, Newly Synthesized I (cid:107) B (cid:98) in Persistent Activation of NF- (cid:107) B
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未磷酸化的新合成 I (cid:107) B (cid:98) 在 NF- (cid:107) B 持续激活中的作用
DOI:
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发表时间:
1996
期刊:
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通讯作者:
Sankar Ghosh
中科院分区:
文献类型:
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作者:
H. Suyang;R. Phillips;I. Douglas;Sankar Ghosh
Stimulation with inducers that cause persistent activation of NF- (cid:107) B results in the degradation of the NF- (cid:107) B inhibitors, I (cid:107) B (cid:97) and I (cid:107) B (cid:98) . Despite the rapid resynthesis and accumulation of I (cid:107) B (cid:97) , NF- (cid:107) B remains induced under these conditions. We now report that I (cid:107) B (cid:98) is also resynthesized in stimulated cells and appears as an unphosphorylated protein. The unphosphorylated I (cid:107) B (cid:98) forms a stable complex with NF- (cid:107) B in the cytosol; however, this binding fails to mask the nuclear localization signal and DNA binding domain on NF- (cid:107) B, and the I (cid:107) B (cid:98) –NF- (cid:107) B complex enters the nucleus. It appears therefore that during prolonged stimulation, I (cid:107) B (cid:98) functions as a chaperone for NF- (cid:107) B by protecting it from I (cid:107) B (cid:97) and allowing it to be transported to the nucleus. The transcription factor NF- (cid:107) B is a ubiquitously expressed transcription factor that plays an important role in the induc- ible expression of a large number of