βTrCP-Mediated Proteolysis of NF-κB1 p105 Requires Phosphorylation of p105 Serines 927 and 932
By V. Lang, J. Janzen, Gregory Zvi Fischer, Y. Soneji, S. Beinke, A. Salmeron, H. Allen, Ronald T. Hay, Y. Ben‐Neriah, S. Ley. Molecular and Cellular Biology, 2003
131 citations recorded by the source corpus.
Subfields: Cancer Research, Immunology
View Paper: https://www.semanticscholar.org/paper/617ddf9f9fd1cb517ed050597ecd475d48248b48
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Citations in the corpus
- Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Unlike p100, IKKb is the p105 kinase and has been shown to phosphorylate Ser-927 and Ser-932, which form the SCF-bTrCP binding site (Orian et al., 2000; Lang et al., 2003) (Figure 3; Table 3).”
- NF-κB1 p105 Negatively Regulates TPL-2 MEK Kinase Activity (2003, background): “TNF- stimulation of p105 proteolysis is triggered by IKK complex phosphorylation of the destruction box in the p105 PEST region (19, 28).”
- The Regulation of NF-κB Subunits by Phosphorylation (2016, background): “Phosphorylation of p105 at S927 and S932 by IKKβ generates a high affinity binding site for βTrCP, the receptor for an SCF-type E3 ubiquitin ligase [15,17] which triggers the ubiquitination of p105 at multiple lysine residues [18].”