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p75 neurotrophin receptor reduces ligand‐induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation
Author(s) -
Makkerh Joe P S,
Ceni Claire,
Auld Daniel S,
Vaillancourt François,
Dorval Genevieve,
Barker Philip A
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400503
Subject(s) - trk receptor , tropomyosin receptor kinase a , low affinity nerve growth factor receptor , tropomyosin receptor kinase b , internalization , neurotrophin , receptor , microbiology and biotechnology , tropomyosin receptor kinase c , biology , neurotrophic factors , biochemistry , platelet derived growth factor receptor , growth factor
Target‐derived neurotrophins regulate neuronal survival and growth by interacting with cell‐surface tyrosine kinase receptors. The p75 neurotrophin receptor (p75NTR) is coexpressed with Trk receptors in long‐range projection neurons, in which it facilitates neurotrophin binding to Trk and enhances Trk activity. Here, we show that TrkA and TrkB receptors undergo robust ligand‐dependent ubiquitination that is dependent on activation of the endogenous Trk activity of the receptors. Coexpression of p75NTR attenuated ubiquitination of TrkA and TrkB and delayed nerve growth factor‐induced TrkA receptor internalization and receptor degradation. These results indicate that p75NTR may prolong cell‐surface Trk‐dependent signalling events by negatively regulating receptor ubiquitination.