CaMKIIα enhances the desensitization of NR2B-containing NMDA receptors by an autophosphorylation-dependent mechanism
作者： Suzanne Sessoms-Sikes , Yumiko Honse , David M. Lovinger , Roger J. Colbran
DOI: 10.1016/J.MCN.2005.01.006
关键词: Long-term potentiation 、 Postsynaptic density 、 NMDA receptor 、 Autophosphorylation 、 Cell biology 、 Synaptic plasticity 、 Biology 、 Neuroscience 、 BAPTA 、 Ca2+/calmodulin-dependent protein kinase 、 Glutamate receptor
摘要: Abstract Long-term potentiation or depression of synaptic function often requires Ca 2+ influx via NMDA-type glutamate receptors (NMDARs) and changes in the autophosphorylation /calmodulin-dependent protein kinase II (CaMKII) at Thr 286 . Autophosphorylated CaMKII binds directly to NMDAR subunits, co-localizes with NMDARs postsynaptic density, phosphorylates NR2B subunits Ser 1303 Here, we demonstrate that CaMKIIα enhances extent and/or rate desensitization NMDA-induced macroscopic currents HEK293 cells co-expressing either NR1 011 101 splice variants, without significantly changing other current parameters. In contrast, containing NR2A place is decreased by co-expression CaMKIIα. Kinases harboring K42R (inactive kinase) T286A (autophosphorylation-deficient) mutations are defective enhancing NR1/NR2B channels. addition, CaMKII-dependent enhancement channel abrogated intracellular loading BAPTA. These data suggest a novel mechanism for -dependent negative-feedback regulation NR2B-containing activity- autophosphorylation-dependent manner may modulate NMDAR-mediated plasticity.
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