SUMOylation and phosphorylation of GluK2 regulate kainate receptor trafficking and synaptic plasticity
Publication date
2012Author
Chamberlain, S.E.Gonzàlez-Gonzàlez, I.M.
Wilkinson, K.A.
Konopacki, F.A.
Kantamneni, Sriharsha
Henley, J.M.
Mellor, J.R.
Keyword
AnimalsExcitatory postsynaptic potentials
HEK293 cells
Humans
Mossy fibers
Neuronal plasticity
Organ culture techniques
Patch-clamp techniques
Phosphorylation
Protein transport
Rats
Wistar
Receptors
Kainic acid
Sumoylation
Synaptic transmission
Transfection
REF 2014
Peer-Reviewed
YesOpen Access status
closedAccess
Metadata
Show full item recordAbstract
Phosphorylation or SUMOylation of the kainate receptor (KAR) subunit GluK2 have both individually been shown to regulate KAR surface expression. However, it is unknown whether phosphorylation and SUMOylation of GluK2 are important for activity-dependent KAR synaptic plasticity. We found that protein kinase C-mediated phosphorylation of GluK2 at serine 868 promotes GluK2 SUMOylation at lysine 886 and that both of these events are necessary for the internalization of GluK2-containing KARs that occurs during long-term depression of KAR-mediated synaptic transmission at rat hippocampal mossy fiber synapses. Conversely, phosphorylation of GluK2 at serine 868 in the absence of SUMOylation led to an increase in KAR surface expression by facilitating receptor recycling between endosomal compartments and the plasma membrane. Our results suggest a role for the dynamic control of synaptic SUMOylation in the regulation of KAR synaptic transmission and plasticity.Version
No full-text in the repositoryCitation
Chamberlain SE, Gonzalez-Gonzalez IM, Wilkinson KA et al (2012) SUMOylation and phosphorylation of GluK2 regulate kainate receptor trafficking and synaptic plasticity. Nature Neuroscience. 15(6): 845-852.Link to Version of Record
https://doi.org/10.1038/nn.3089Type
Articleae974a485f413a2113503eed53cd6c53
https://doi.org/10.1038/nn.3089