4月22日,，國(guó)際著名雜志《自然—神經(jīng)科學(xué)》Nature Neuroscience上刊登了國(guó)外研究人員的最新研究成果“SUMOylation and phosphorylation of GluK2 regulate kainate receptor trafficking and synaptic plasticity”,，文章中，來(lái)自英國(guó)布里斯托爾大學(xué)的神經(jīng)學(xué)家們?cè)谘芯恐邪l(fā)現(xiàn)了一種被稱為SUMO的蛋白對(duì)減少或增強(qiáng)大腦神經(jīng)細(xì)胞保護(hù)機(jī)制的化學(xué)過(guò)程起重要調(diào)控作用,。這種關(guān)鍵蛋白在心力衰竭或癲癇發(fā)作過(guò)程中能夠激活保護(hù)神經(jīng)細(xì)胞免受損傷,，并且它還調(diào)控大腦神經(jīng)細(xì)胞間的信息傳遞,。這項(xiàng)研究將有可能推動(dòng)開(kāi)發(fā)出中風(fēng)和癲癇的治療新策略,。
研究人員證實(shí)這些關(guān)鍵的SUMO蛋白通過(guò)對(duì)大腦活動(dòng)水平生成精細(xì)的反應(yīng)而調(diào)控了紅藻氨酸受體（Kainate receptor， KAR）傳輸?shù)男盘?hào)量,。紅藻氨酸受體對(duì)神經(jīng)細(xì)胞間的溝通起重要作用,，受體激活可導(dǎo)致癲癇發(fā)作和神經(jīng)細(xì)胞死亡。
布里斯托爾大學(xué)醫(yī)學(xué)院的Jack Mellor指出：“紅藻氨酸受體是一組非常重要的蛋白,，已知與包括癲癇在內(nèi)的大量疾病有關(guān),。這些研究發(fā)現(xiàn)為我們提供了SUMO和紅藻氨酸受體之間的聯(lián)系，增進(jìn)了我們對(duì)于神經(jīng)細(xì)胞保護(hù)自身免于過(guò)度和不正?；顒?dòng)機(jī)制的理解,。”（生物谷Bioon.com）
doi:10.1038/nn.3089
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SUMOylation and phosphorylation of GluK2 regulate kainate receptor trafficking and synaptic plasticity
Sophie E L Chamberlain, Inmaculada M González-González, Kevin A Wilkinson, Filip A Konopacki, Sriharsha Kantamneni, Jeremy M Henley & Jack R Mellor
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.
