Li Deng

TL;DR: The purification and identification of TRIKA2, which is composed of TAK1, TAB1 and TAB2, a protein kinase complex previously implicated in IKK activation through an unknown mechanism, indicate that ubiquitination has an important regulatory role in stress response pathways, including those of IKK and JNK.

TL;DR: It is found that TRAF6, a RING domain protein, functions together with Ubc13/Uev1A to catalyze the synthesis of unique polyubiquitin chains linked through lysine-63 (K63) of ubiquitin.

TL;DR: The results reveal the biochemical mechanism underlying the essential signaling function of NEMO and provide direct evidence that signal-induced site-specific ubiquitination of RIP1 is required for IKK activation.

TL;DR: Evidence is presented that TAB2 and TAB3 are receptors that bind preferentially to lysine 63-linked polyubiquitin chains through a highly conserved zinc finger (ZnF) domain, which indicates that polyubanquitin binding domains represent a new class of signaling domains that regulate protein kinase activity through a nonproteolytic mechanism.

TL;DR: Evidence is presented that TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by BCL10 and MALT1, and a small fraction of these proteins form high molecular weight oligomers, which culminates in NF-kappaB activation in T lymphocytes.