IndraLab

Statements

IKK_complex phosphorylates CYLD on S436. 4 / 4
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rlimsp
"Notably, among the four reported IKK phosphorylation sites [34] (S418, S422, S432 and S436) that may create two putative β-TRCP binding motifs (Figure 3E), mutating both phospho-degrons of CYLD abolished the interaction between CYLD and β-TRCP (Figures 3D-E)."
24961988
rlimsp
"These results support the notion that phosphorylation of CYLD by IKK at Ser432 and Ser436 is associated with β-TRCP-mediated poly-ubiquitination and subsequent degradation of CYLD."
24961988
rlimsp
"Here, we report that SCFβ-TRCP regulates the ubiquitination and degradation of CYLD, a process dependent on prior phosphorylation of CYLD at Ser432/Ser436 by IKK."
24961988
sparser
"These results support the notion that phosphorylation of CYLD by IKK at Ser432 and Ser436 is associated with β-TRCP-mediated poly-ubiquitination and subsequent degradation of CYLD."
24961988