SCF-beta-TRCP binds p-7S-p100 in active NIK:p-S176,180-IKKA dimer:p-7S-p100:RELB

Stable Identifier
Reaction [binding]
Homo sapiens
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Phosphorylated C-terminal serines 866, 870 and 872 in NFKB2 creates binding site for beta-TRCP (beta-transducin repeat-containing protein), the receptor subunit of a SCF-type of E3 ubiquitin ligase, SCF beta-TRCP (Liang et al. 2006). The SKP1-CUL1-F-box (SCF) ubiquitin E3 ligase superfamily is the largest family of cullin-RING ligases, with interchangeable F-box proteins orchestrating the trafficking proteins for ubiquitination and degradation (Weathington & Mallampalli 2013). Beta-TRCP is an F-box protein that contains two domains, an F-box motif that binds SKP1 and allows assembly into SKP1-CUL1 complexes and a second protein-protein interaction domain that interacts with phosphorylated serines in NFKB2 (Bai et al. 1996, Skowyra et al. 1997, Patton et al. 1998).

Literature References
PubMed ID Title Journal Year
8706131 SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box

Hofmann, K, Goebl, M, Sen, P, Ma, L, Bai, C, Elledge, SJ, Harper, JW

Cell 1996
16303288 beta-TrCP binding and processing of NF-kappaB2/p100 involve its phosphorylation at serines 866 and 870

Liang, C, Sun, SC, Zhang, M

Cell. Signal. 2006
15340381 The SCF ubiquitin ligase: insights into a molecular machine

Cardozo, T, Pagano, M

Nat. Rev. Mol. Cell Biol. 2004
9346238 F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex

Skowyra, D, Craig, KL, Elledge, SJ, Tyers, M, Harper, JW

Cell 1997
Orthologous Events
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