Dimerization-dependent block of the proapoptotic effect of p75(NTR)

Détails

ID Serval
serval:BIB_477E220107B7
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Dimerization-dependent block of the proapoptotic effect of p75(NTR)
Périodique
Journal of Neuroscience Research
Auteur(s)
Wang  J. J., Rabizadeh  S., Tasinato  A., Sperandio  S., Ye  X., Green  M., Assa-Munt  N., Spencer  D., Bredesen  D. E.
ISSN
0360-4012 (Print)
Statut éditorial
Publié
Date de publication
06/2000
Volume
60
Numéro
5
Pages
587-93
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jun 1
Résumé
The biochemical mechanism by which neurons become dependent on neurotrophins for survival is unknown. We found previously that the common neurotrophin receptor, p75(NTR), is a mediator of neurotrophin dependence and that this effect requires a novel type of domain dubbed a neurotrophin dependence domain. We report here that, in contrast to other proapoptotic receptors such as Fas, apoptosis induction by p75(NTR) requires monomerization, with dimerization inhibiting the effect. Blocking the proapoptotic effect of the monomer by dimerization requires a distinct domain that lies at the carboxyterminus of p75(NTR). These results define a novel type of domain required for inhibiting apoptosis induction by p75(NTR).
Mots-clé
Apoptosis/drug effects/*physiology Carrier Proteins/drug effects/*metabolism Cells, Cultured Cross-Linking Reagents/pharmacology Dimerization Humans Nerve Tissue Proteins/drug effects/*metabolism Neurotrophin 3/pharmacology Protein Structure, Tertiary/drug effects/physiology *Receptors, Growth Factor Receptors, Nerve Growth Factor/drug effects/*metabolism Selective Estrogen Receptor Modulators/pharmacology Tacrolimus/analogs & derivatives/pharmacology Tamoxifen/pharmacology Transfection
Pubmed
Web of science
Création de la notice
29/01/2008 9:44
Dernière modification de la notice
03/03/2018 16:50
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