Modulation of GluK2a Subunit-containing Kainate Receptors by 14-3-3 Proteins
Year: 2013
Type: article
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. Background: The mechanisms underlying slow kinetics of the kainate receptor-mediated EPSCs are not totally understood. Results: Phosphorylation-dependent binding of 14-3-3 proteins to GluK2a subunits modulates the biophysical property of GluK2a-containing kainate receptors. Conclusion: 14-3-3 is an important regulator of GluK2a-containing kainate receptors. Significance: The dynamically regulated 14-3-3·GluK2a protein complex may contribute to the diverse functions of kainate receptors in synaptic signaling.
Source: Journal of Biological Chemistry
Authors: Changcheng Sun, Haifa Qiao, Qin Zhou, Yan Wang, Yuying Wu, Yi Zhou, Yong Li
Institutions: Shanghai Jiao Tong University, Florida State University
Language: English
Subfield: Cellular and Molecular Neuroscience
Field: Neuroscience
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2048825451