Synaptic clustering of PSD-95 is regulated by c-Abl through tyrosine phosphorylation

Karen Perez de Arce, Lorena Varela-Nallar, Olivia Farias, Alejandra Cifuentes, Paulina Bull, Brian A. Couch, Anthony J. Koleske, Nibaldo C. Inestrosa, Alejandra R. Alvarez

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

38 Citas (Scopus)

Resumen

The c-Abl tyrosine kinase is present in mouse brain synapses, but its precise synaptic function is unknown.Wefound that c-Abl levels in the rat hippocampus increase postnatally, with expression peaking at the first postnatal week. In 14 d in vitro hippocampal neuron cultures, c-Abl localizes primarily to the postsynaptic compartment, in which it colocalizes with the postsynaptic scaffold protein postsynaptic density protein-95 (PSD-95) in apposition to presynaptic markers. c-Abl associates with PSD-95, and chemical or genetic inhibition of c-Abl kinase activity reduces PSD-95 tyrosine phosphorylation, leading to reduced PSD-95 clustering and reduced synapses in treated neurons. c-Abl can phosphorylate PSD-95 on tyrosine 533, and mutation of this residue reduces the ability of PSD-95 to cluster at postsynaptic sites. Our results indicate that c-Abl regulates synapse formation by mediating tyrosine phosphorylation and clustering of PSD-95.

Idioma originalInglés
Páginas (desde-hasta)3728-3738
Número de páginas11
PublicaciónJournal of Neuroscience
Volumen30
N.º10
DOI
EstadoPublicada - 10 mar 2010

Áreas temáticas de ASJC Scopus

  • Neurociencia (todo)

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