Synaptic Clustering of PSD-95 Is Regulated by c-Abl through Tyrosine Phosphorylation

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dc.contributor.authorPerez de Arce, Karen
dc.contributor.authorVarela Nallar, Lorena
dc.contributor.authorFarias, Olivia
dc.contributor.authorCifuentes, Alejandra
dc.contributor.authorBull, Paulina
dc.contributor.authorCouch, Brian A.
dc.contributor.authorKoleske, Anthony J.
dc.contributor.authorInestrosa, Nibaldo C.
dc.contributor.authorAlvarez, Alejandra R.
dc.date.accessioned2024-01-10T12:09:03Z
dc.date.available2024-01-10T12:09:03Z
dc.date.issued2010
dc.description.abstractThe c-Abl tyrosine kinase is present in mouse brain synapses, but its precise synaptic function is unknown. We found 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.
dc.description.funderFondo Nacional de Desarrollo Cientifico y Tecnologico
dc.description.funderFondo de Investigacion Avanzada en Areas Prioritarias - Biomedicine
dc.description.funderMillennium Institute for Fundamental and Applied Biology
dc.description.funderMejoramiento de la Calidad y la Equidad de la Educacion Superior-Pontificia Universidad Catolica de Chile
dc.description.funderNational Institutes of Health
dc.description.funderNATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
dc.format.extent11 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1523/JNEUROSCI.2024-09.2010
dc.identifier.eissn1529-2401
dc.identifier.issn0270-6474
dc.identifier.pubmedidMEDLINE:20220006
dc.identifier.urihttps://doi.org/10.1523/JNEUROSCI.2024-09.2010
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/76453
dc.identifier.wosidWOS:000275400000019
dc.information.autorucCiencias Biológicas;Bull P;S/I;99734
dc.information.autorucCiencias Biológicas;Cifuentes A;S/I;142391
dc.information.autorucCiencias Biológicas;Farías O;S/I;132625
dc.information.autorucCiencias Biológicas;Inestrosa N;S/I;99331
dc.information.autorucCiencias Biológicas;Pérez de Arce K;S/I;18209
dc.information.autorucCiencias Biológicas;Varela-Nallar L;S/I;127946
dc.information.autorucCiencias Biológicas;Álvarez A;S/I;83681
dc.issue.numero10
dc.language.isoen
dc.nota.accesoSin adjunto
dc.pagina.final3738
dc.pagina.inicio3728
dc.publisherSOC NEUROSCIENCE
dc.revistaJOURNAL OF NEUROSCIENCE
dc.rightsregistro bibliográfico
dc.subjectPOSTSYNAPTIC DENSITY PROTEINS
dc.subjectDENDRITIC SPINE MORPHOLOGY
dc.subjectLONG-TERM POTENTIATION
dc.subjectDEPENDENT REGULATION
dc.subjectRECEPTOR FUNCTION
dc.subjectKINASE-II
dc.subjectFAMILY
dc.subjectDOMAIN
dc.subjectBRAIN
dc.subjectACTIN
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleSynaptic Clustering of PSD-95 Is Regulated by c-Abl through Tyrosine Phosphorylation
dc.typeartículo
dc.volumen30
sipa.codpersvinculados99734
sipa.codpersvinculados142391
sipa.codpersvinculados132625
sipa.codpersvinculados99331
sipa.codpersvinculados18209
sipa.codpersvinculados127946
sipa.codpersvinculados83681
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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