Metabotropic glutamate receptor-initiated translocation of protein kinase p90rsk to polyribosomes:: A possible factor regulating synaptic protein synthesis
Metabotropic glutamate receptor-initiated translocation of protein kinase p90rsk to polyribosomes:: A possible factor regulating synaptic protein synthesis
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DOI：
10.1073/pnas.95.25.15078
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发表时间：
1998-12-08
影响因子：
11.1
通讯作者：
Weiler, IJ
中科院分区：
文献类型：
--
作者：
Angenstein, F;Greenough, WT;Weiler, IJ
维持持久的突触功效变化需要蛋白质合成。我们在这里报告的机制，可能会影响翻译控制在单突触的水平。海马脑片中代谢型谷氨酸受体的刺激诱导多功能激酶p90 rsk向多聚核糖体的快速蛋白激酶C依赖性易位;同时，至少6种多聚核糖体结合蛋白的磷酸化增强。多聚核糖体结合蛋白包括p90 rsk激活激酶ERK-2和已知的p90 rsk底物糖原合成酶激酶3 β，其通过真核起始因子2B调节翻译效率。因此，代谢型谷氨酸受体刺激可以通过p90 rsk移位到核糖体来诱导突触活性依赖性翻译。
Maintenance of lasting synaptic efficacy changes requires protein synthesis. We report here a mechanism that might influence translation control at the level of the single synapse. Stimulation of metabotropic glutamate receptors in hippocampal slices induces a rapid protein kinase C-dependent translocation of multifunction kinase p90rsk to polyribosomes; concomitantly, there is enhanced phosphorylation of at least six polyribosome binding proteins. Among the polyribosome bound proteins are the p90rsk-activating kinase ERK-2 and a known p90rsk substrate, glycogen synthase kinase 3 beta, which regulates translation efficiency via eukaryotic initiation factor 2B. Thus metabotropic glutamate receptor stimulation could induce synaptic activity-dependent translation via translocation of p90rsk to ribosomes.