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Updated: Aug 22, 2026

An Improved Protocol to Purify and Directly Mono-Biotinylate Recombinant BDNF in a Tube for Cellular Trafficking Studies in Neurons
Published on: July 11, 2020
c-Cbl binds to tyrosine-phosphorylated neurotrophin receptor p75 and induces its ubiquitination
Thomas Ohrt1, Annalisa Mancini, Teruko Tamura
1Institute for Biophysics, University of Technology, 01307 Dresden, Germany.
Abstract:
The p75 neurotrophin receptor (p75NTR) has dual functions in cell survival and cell death but its intracellular signalling pathways are not understood. Here we describe that in rat brain and in pervanadate-stimulated PCNA and HEK293 cells p75NTR is phosphorylated at a single tyrosine residue within the cytosolic C-terminus. Phosphorylated tyrosine 308 constitutes a binding site for the ubiquitin ligase c-Cbl. This interaction is a prerequisite for ubiquitination of p75NTR. Our data suggest a c-Cbl-dependent ubiquitination of p75NTR involved in the regulation of p75NTR signalling.
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