Abstract:
:Mutant I1A cells, lacking IL-1 receptor-associated kinase (IRAK) mRNA and protein, have been used to study the involvement of IRAK in NFkappaB and c-Jun N-terminal kinase (JNK) activation. A series of IRAK deletion constructs were expressed in I1A cells, which were then tested for their ability to respond to IL-1. Both the N-terminal death domain and the C-terminal region of IRAK are required for IL-1-induced NFkappaB and JNK activation, whereas the N-proximal undetermined domain is required for the activation of NFkappaB but not JNK. The phosphorylation and ubiquitination of IRAK deletion mutants correlate tightly with their ability to activate NFkappaB in response to IL-1, but IRAK can mediate IL-1-induced JNK activation without being phosphorylated. These studies reveal that the IL-1-induced signaling pathways leading to NFkappaB and JNK activation diverge either at IRAK or at a point nearer to the receptor.
journal_name
Proc Natl Acad Sci U S Aauthors
Li X,Commane M,Jiang Z,Stark GRdoi
10.1073/pnas.071054198keywords:
subject
Has Abstractpub_date
2001-04-10 00:00:00pages
4461-5issue
8eissn
0027-8424issn
1091-6490pii
071054198journal_volume
98pub_type
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