IndraLab

Statements


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sparser
"Here we demonstrate that E3 ligase Itch and deubiquitinase Cyld form a complex via the interaction through ‘WW-PPXY’ motifs."

sparser
"E3 ligase Itch and deubiquitinase CYLD form a complex that cleaves lysine (Lys) 63-linked ubiquitin chains and catalyze Lys48-linked ubiquitination on the kinase Tak1, which is a common substrate for these two proteins, thereby contributing to decreased inflammatory signalling [ xref ]."

sparser
"Recently, it has been demonstrated that E3 ligase ITCH and CYLD formed a complex which can sequentially cleave K63-linked ubiquitin-chain and catalyzes K48-linked ubiquitination to deactivate TAK1 and terminate NF-κB signaling (Ahmed et al., xref ), providing an example of how K48 and K63-linked ubiquitinations are closely linked and can be differentially utilized to control kinase activation and deactivation."