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Article

Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

Neuron - 16 Apr 2009

Vilar Marçal, Charalampopoulos Ioannis, Kenchappa Rajappa S, Simi Anastasia, Karaca Esra, Reversi Alessandra, Choi Soyoung, Bothwell Mark, Mingarro Ismael, Friedman Wilma J, Schiavo Giampietro, Bastiaens Philippe I H, Verveer Peter J, Carter Bruce D, Ibáñez Carlos F

Abstract excerpt

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Neurotrophins interact with dimers of the p75 neurotrophin receptor (p75(NTR)), but the mechanism of receptor activation has remained elusive. Here, we show that p75(NTR) forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys(257) in its transmembrane domain....

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Identifiers

PMID: 19376068
DOI: 10.1016/j.neuron.2009.02.020
PMCID: PMC2810632

Genes

MAG
NGF

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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