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

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

dc.contributor.author	Vilar, Marçal
dc.contributor.author	Charalampopoulos, Ioannis
dc.contributor.author	Kenchappa, Rajappa S.
dc.contributor.author	Simi, Anastasia
dc.contributor.author	Karaca, Esra
dc.contributor.author	Reversi, Alessandra
dc.contributor.author	Choi, Soyoung
dc.contributor.author	Bothwell, Mark
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Friedman, Wilma J.
dc.contributor.author	Schiavo, Giampietro
dc.contributor.author	Bastiaens, Philippe I.H.
dc.contributor.author	Verveer, Peter J.
dc.contributor.author	Carter, Bruce D.
dc.contributor.author	Ibañez, Carlos F.
dc.date.accessioned	2016-12-01T16:05:32Z
dc.date.available	2016-12-01T16:05:32Z
dc.date.issued	2009
dc.identifier.citation	Vilar, Marçal Charalampopoulos, Ioannis Kenchappa, Rajappa S. Simi, Anastasia Karaca, Esra Reversi, Alessandra Choi, Soyoung Bothwell, Mark Mingarro Muñoz, Ismael Friedman, Wilma J. Schiavo, Giampietro Bastiaens, Philippe I.H. Verveer, Peter J. Carter, Bruce D. Ibañez, Carlos F. 2009 Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers Neuron 62 1 72 83
dc.identifier.uri	http://hdl.handle.net/10550/56221
dc.description.abstract	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. Mutation of Cys(257) abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75(NTR)/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p75(NTR). FRET experiments revealed a close association of p75(NTR) intracellular domains that was transiently disrupted by conformational changes induced upon NGF binding. Although mutation of Cys(257) did not alter the oligomeric state of p75(NTR), the mutant receptor was no longer able to propagate conformational changes to the cytoplasmic domain upon ligand binding. We propose that neurotrophins activate p75(NTR) by a mechanism involving rearrangement of disulphide-linked receptor subunits.
dc.language.iso	eng
dc.relation.ispartof	Neuron, 2009, vol. 62, num. 1, p. 72-83
dc.subject	Proteïnes
dc.subject	Neurones
dc.subject	Receptors neurals
dc.title	Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers
dc.type	journal article	es_ES
dc.date.updated	2016-12-01T16:05:33Z
dc.identifier.doi	10.1016/j.neuron.2009.02.020
dc.identifier.idgrec	053687
dc.rights.accessRights	open access	es_ES