Abstract:IL-1 is a proinflammatory cytokine that signals through a receptor complex of two different transmembrane chains to generate multiple cellular responses, including activation of the transcription factor NF-kappaB. Here we show that MyD88, a previously described protein of unknown function, is recruited to the IL-1 receptor complex following IL-1 stimulation. MyD88 binds to both IRAK (IL-1 receptor-associated kinase) and the heterocomplex (the signaling complex) of the two receptor chains and thereby mediates t… Show more
“…Whether it functions like TRADD is not known negative which blocks NF-kB activation by IL-1, but not by TNF. Both the N-and C-terminal fragments of MyD88 were observed to interact with IRAK (Wesche et al, 1997a). Formation of MyD88 homodimers, mediated via the death domain, was observed as well.…”
Section: Egr-1 ±Modulation Of Lineage Speci®c DI Erentiation and Rolementioning
confidence: 84%
“…Several reports in the last year have identi®ed MyD88 as an adapter that recruits IRAK to the IL-1 receptor complex Wesche et al, 1997a;Muzio et al, 1997) (Figure 3). It was shown that following IL-1 stimulation MyD88 binds to both IRAK and the IL-1R/IL-1AcP receptor complex, thereby linking IRAK to the receptor.…”
Section: Egr-1 ±Modulation Of Lineage Speci®c DI Erentiation and Rolementioning
“…Whether it functions like TRADD is not known negative which blocks NF-kB activation by IL-1, but not by TNF. Both the N-and C-terminal fragments of MyD88 were observed to interact with IRAK (Wesche et al, 1997a). Formation of MyD88 homodimers, mediated via the death domain, was observed as well.…”
Section: Egr-1 ±Modulation Of Lineage Speci®c DI Erentiation and Rolementioning
confidence: 84%
“…Several reports in the last year have identi®ed MyD88 as an adapter that recruits IRAK to the IL-1 receptor complex Wesche et al, 1997a;Muzio et al, 1997) (Figure 3). It was shown that following IL-1 stimulation MyD88 binds to both IRAK and the IL-1R/IL-1AcP receptor complex, thereby linking IRAK to the receptor.…”
Section: Egr-1 ±Modulation Of Lineage Speci®c DI Erentiation and Rolementioning
“…All TLRs except TLR3 and TLR4 have been shown to require MyD88 for effective downstream signaling, dividing the TLR family between MyD88-dependent and MyD88-independent members [15]. In the case of pathogenic invading, MyD88 was up-regulated to enhance the activation of downstream transcription factors, such as NF-kB and AP-1 [16]. In the MyD88-independent TLR signaling pathway, TLR3 induce the activation of the IFN-b promoter, a function unimpaired by the knockdown of MyD88 [17].…”
“…Unexpectedly, we found two novel truncated forms of Myd88 lacking DD domain, CgMyD88-T1 and CgMyD88-T2. Both CgMyD88Ts contain the conserved TIR domain, which has previously been proved to be required for mediating TLR/MyD88 heterodimerization to activate the followed signaling transduction [19].…”
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.