Protein kinase CK2 in postsynaptic densities: Phosphorylation of PSD-95/SAP90 and NMDA receptor regulation
Author
dc.contributor.author
Soto, Dagoberto
Author
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Pancetti, Floria
Author
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Marengo, Juan José
Author
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Sandoval, Mauricio
Author
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Sandoval, Rodrigo
Author
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Orrego, Fernando
Author
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Wyneken, Ursula
Admission date
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2019-03-11T12:56:55Z
Available date
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2019-03-11T12:56:55Z
Publication date
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2004
Cita de ítem
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Biochemical and Biophysical Research Communications, Volumen 322, Issue 2, 2018, Pages 542-550
Identifier
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0006291X
Identifier
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10.1016/j.bbrc.2004.07.158
Identifier
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https://repositorio.uchile.cl/handle/2250/164701
Abstract
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Protein kinase CK2 (CK2) is highly expressed in rat forebrain where its function is not well understood. Subcellular distribution studies showed that the catalytic subunit of CK2 (CK2α) was enriched in postsynaptic densities (PSDs) by 68%. We studied the putative role of CK2 activity on N-methyl-d-aspartate receptor (NMDAR) function using isolated, patch-clamped PSDs in the presence of 2 mM extracellular Mg 2+. The usual activation by phosphorylation of the NMDARs in the presence of ATP was inhibited by the selective CK2 inhibitor 5,6-dichloro-1-β-ribofuranosyl benzimidazole (DRB). This inhibition was voltage-dependent, i.e., 100% at positive membrane potentials, while at negative potentials, inhibition was incomplete. Endogenous CK2 substrates were characterized by their ability to use GTP as a phosphoryl donor and susceptibility to inhibition by DRB. Immunoprecipitation assays and 2D gels indicated that PSD-95/SAP90, the NMDAR scaffolding protein, was a CK2 substrate, while the NR2A/