IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2.

@article{Suzuki1999IkappaBalphaUI,
  title={IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2.},
  author={Hiromi Suzuki and Tomoki Chiba and Makio Kobayashi and Masakazu Takeuchi and Toshiharu Suzuki and Arata Ichiyama and Tsuneo Ikenoue and Masao Omata and Kiyoshi Furuichi and Keiji Tanaka},
  journal={Biochemical and biophysical research communications},
  year={1999},
  volume={256 1},
  pages={127-32}
}
Destruction of the transcriptional inhibitor IkappaB by the ubiquitin (Ub) system is required for signal-dependent activation of the multifunctional transcriptional factor NF-kappaB, but details of this ubiquitination are largely unknown. We report here that the IkappaBalpha-ubiquitin ligase (IkappaBalpha-E3) is an SCF-like complex containing Skp1, cullin-1, and two homologous F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2. Intriguingly, all these components are cooperatively recruited to… CONTINUE READING
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