Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling

Détails

ID Serval
serval:BIB_963DF8948570
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling
Périodique
FEBS Letters
Auteur⸱e⸱s
Kaufmann  M., Bozic  D., Briand  C., Bodmer  J. L., Zerbe  O., Kohl  A., Tschopp  J., Grutter  M. G.
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
09/2002
Volume
527
Numéro
1-3
Pages
250-4
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Sep 11
Résumé
Death effector domains (DEDs) are protein-protein interaction domains found in the death inducing signaling complex (DISC). Performing a structure-based alignment of all DED sequences we identified a region of high diversity in alpha-helix 3 and propose a classification of DEDs into class I DEDs typically containing a stretch of basic residues in the alpha-helix 3 region whereas DEDs of class II do not. Functional assays using mutants of Fas-associated death domain revealed that this basic region influences binding and recruitment of caspase-8 and cellular FLICE inhibitor protein to the DISC.
Mots-clé
*Adaptor Proteins, Signal Transducing Amino Acid Sequence Apoptosis/*physiology Binding Sites CASP8 and FADD-Like Apoptosis Regulating Protein Carrier Proteins/*chemistry/genetics/*metabolism Caspase 3 Caspases/metabolism Cells, Cultured Fas-Associated Death Domain Protein Humans *Intracellular Signaling Peptides and Proteins Models, Molecular Molecular Sequence Data Mutation Protein Conformation Protein Structure, Tertiary Signal Transduction
Pubmed
Web of science
Création de la notice
24/01/2008 15:18
Dernière modification de la notice
20/08/2019 14:58
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