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Dimerization‐dependent block of the proapoptotic effect of P75 NTR
Author(s) -
Wang James J.L.,
Rabizadeh Shahrooz,
Tasinato Andrea,
Sperandio Sabina,
Ye Xin,
Green Michael,
AssaMunt Nuria,
Spencer David,
Bredesen Dale E.
Publication year - 2000
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(20000601)60:5<587::aid-jnr3>3.0.co;2-1
Subject(s) - low affinity nerve growth factor receptor , neurotrophin , mediator , receptor , chemistry , microbiology and biotechnology , apoptosis , neurotrophin 3 , neuroscience , biology , neurotrophic factors , biochemistry , brain derived neurotrophic factor
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 . J. Neurosci. Res. 60:587–593, 2000 © 2000 Wiley‐Liss, Inc.