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Multi‐tasking by the p75 neurotrophin receptor: sortilin things out?
Author(s) -
Bronfman Francisca C,
Fainzilber Mike
Publication year - 2004
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.7400219
Subject(s) - low affinity nerve growth factor receptor , endosome , signal transducing adaptor protein , microbiology and biotechnology , receptor , biology , neurotrophin , extracellular , signalling , intracellular , signal transduction , genetics
Signalling by the p75 neurotrophin receptor has been implicated in diverse neuronal responses, including increased differentiation or survival, inhibition of regeneration, and initiation of apoptotic cell death. These numerous roles are matched by, but are not yet correlated with, a multiplicity of extracellular ligands and intracellular interactors. Membrane proteins such as sortilin, a member of the Vps10p family of sorting receptors, and the glycosylphosphatidylinositol‐linked Nogo receptor (NgR) and the associated adaptor lingo 1 have recently been added to the list of p75‐interacting modulators. Other studies have described intramembranal cleavage of p75 and the potential nuclear targeting of cleavage fragments or of the complete receptor after it has been internalized into a putative signalling endosome. These findings suggest that some of the diversity in p75 activities might be due to differential subcellular localization and transport of p75 receptor complexes. We therefore argue that cell‐biology‐driven approaches are now required to make sense of p75 signalling.