Takayoshi Kirisako

TL;DR: Results indicate that LUBAC is involved in the physiological regulation of the canonical NF-κB activation pathway through linear polyubiquitylation of NEMO.

TL;DR: It is reported that a protein complex consisting of two RING finger proteins, HOIL‐1L and HOIP, exhibits ubiquitin polymerization activity by recognizing ubiquitIn moieties of proteins, indicating that the ligase complex possesses a unique feature to assemble a novel head‐to‐tail linear polyubiquitin chain.

TL;DR: It is reported here that not only Cys201, an invariant residue in the heme regulatory motif (HRM), but also His204 is critical for IRP2 degradation, indicating the involvement of these residues in sensing the redox state of theheme iron and in generating the oxidative modification.

TL;DR: It is shown that gliotoxin inhibits signal-induced NF-κB activation by selectively inhibiting LUBAC-mediated linear ubiquitin chain formation.

TL;DR: Results indicate that various mechanisms regulate both the activities and the stability of cullin‐based ligases, as they determine the specificity of the system.