Modulation of GluK2a Subunit-containing Kainate Receptors by 14-3-3 Proteins |
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Authors: | Changcheng Sun Haifa Qiao Qin Zhou Yan Wang Yuying Wu Yi Zhou Yong Li |
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Affiliation: | From the ‡Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China and ;the §Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, Florida 32306 |
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Abstract: | Kainate receptors (KARs) are one of the ionotropic glutamate receptors that mediate excitatory postsynaptic currents (EPSCs) with characteristically slow kinetics. Although mechanisms for the slow kinetics of KAR-EPSCs are not totally understood, recent evidence has implicated a regulatory role of KAR-associated proteins. Here, we report that decay kinetics of GluK2a-containing receptors is modulated by closely associated 14-3-3 proteins. 14-3-3 binding requires PKC-dependent phosphorylation of serine residues localized in the carboxyl tail of the GluK2a subunit. In transfected cells, 14-3-3 binding to GluK2a slows desensitization kinetics of both homomeric GluK2a and heteromeric GluK2a/GluK5 receptors. Moreover, KAR-EPSCs at mossy fiber-CA3 synapses decay significantly faster in the 14-3-3 functional knock-out mice. Collectively, these results demonstrate that 14-3-3 proteins are an important regulator of GluK2a-containing KARs and may contribute to the slow decay kinetics of native KAR-EPSCs. |
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Keywords: | Glutamate Receptors Phosphorylation Protein Kinase C (PKC) Protein/Protein Interactions Receptor Desensitization 14-3-3 Proteins Channel Kinetics Kainate Receptors |
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