MyD88, an adapter protein involved in interleukin-1 signaling.

Détails

Ressource 1Télécharger: 031. Burns et al.pdf (364.74 [Ko])
Etat: Public
Version: de l'auteur
Licence: Non spécifiée
ID Serval
serval:BIB_5FF43594B66A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
MyD88, an adapter protein involved in interleukin-1 signaling.
Périodique
Journal of Biological Chemistry
Auteur(s)
Burns K., Martinon F., Esslinger C., Pahl H., Schneider P., Bodmer J.L., Di Marco F., French L., Tschopp J.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
1998
Volume
273
Numéro
20
Pages
12203-12209
Langue
anglais
Résumé
MyD88 has a modular organization, an N-terminal death domain (DD) related to the cytoplasmic signaling domains found in many members of the tumor necrosis factor receptor (TNF-R) superfamily, and a C-terminal Toll domain similar to that found in the expanding family of Toll/interleukin-1-like receptors (IL-1R). This dual domain structure, together with the following observations, supports a role for MyD88 as an adapter in IL-1 signal transduction; MyD88 forms homodimers in vivo through DD-DD and Toll-Toll interactions. Overexpression of MyD88 induces activation of the c-Jun N-terminal kinase (JNK) and the transcription factor NF-kappaB through its DD. A point mutation in MyD88, MyD88-lpr (F56N), which prevents dimerization of the DD, also blocks induction of these activities. MyD88-induced NF-kappaB activation is inhibited by the dominant negative versions of TRAF6 and IRAK, which also inhibit IL-1-induced NF-kappaB activation. Overexpression of MyD88-lpr or MyD88-Toll (expressing only the Toll domain) acted to inhibit IL-1-induced NF-kappaB and JNK activation in a 293 cell line overexpressing the IL-1RI. MyD88 coimmunoprecipitates with the IL-1R signaling complex in an IL-1-dependent manner.
Mots-clé
Adaptor Proteins, Signal Transducing, Animals, Antigens, Differentiation, Calcium-Calmodulin-Dependent Protein Kinases/metabolism, Cell Line, Dimerization, Enzyme Activation, Humans, Interleukin-1/metabolism, JNK Mitogen-Activated Protein Kinases, Mice, Mitogen-Activated Protein Kinases, Myeloid Differentiation Factor 88, NF-kappa B/metabolism, Proteins/metabolism, Receptors, Immunologic, Recombinant Proteins/metabolism, Signal Transduction
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:19
Dernière modification de la notice
18/01/2020 8:09
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