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Dimerization-dependent block of the proapoptotic effect of p75(NTR).
- Source :
-
Journal of neuroscience research [J Neurosci Res] 2000 Jun 01; Vol. 60 (5), pp. 587-93. - Publication Year :
- 2000
-
Abstract
- 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).<br /> (Copyright 2000 Wiley-Liss, Inc.)
- Subjects :
- Apoptosis drug effects
Carrier Proteins drug effects
Cells, Cultured
Cross-Linking Reagents pharmacology
Dimerization
Humans
Nerve Tissue Proteins drug effects
Neurotrophin 3 pharmacology
Protein Structure, Tertiary drug effects
Protein Structure, Tertiary physiology
Receptors, Nerve Growth Factor drug effects
Selective Estrogen Receptor Modulators pharmacology
Tacrolimus analogs & derivatives
Tacrolimus pharmacology
Tamoxifen pharmacology
Transfection
Apoptosis physiology
Carrier Proteins metabolism
Nerve Tissue Proteins metabolism
Receptors, Growth Factor
Receptors, Nerve Growth Factor metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0360-4012
- Volume :
- 60
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of neuroscience research
- Publication Type :
- Academic Journal
- Accession number :
- 10820429
- Full Text :
- https://doi.org/10.1002/(SICI)1097-4547(20000601)60:5<587::AID-JNR3>3.0.CO;2-1