代谢型谷氨酸受体引发蛋白激酶p90rsk向多核糖体的转位：调节突触蛋白合成的一个可能因素。
Metabotropic glutamate receptor-initiated translocation of protein kinase p90rsk to polyribosomes: a possible factor regulating synaptic protein synthesis.
作者信息
Angenstein F, Greenough W T, Weiler I J
机构信息
Department of Beckman Institute, University of Illinois, Urbana-Champaign, IL 61801, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):15078-83. doi: 10.1073/pnas.95.25.15078.
Abstract
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 3beta, 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.
摘要
维持持久的突触效能变化需要蛋白质合成。我们在此报告一种可能在单个突触水平影响翻译控制的机制。海马切片中促代谢型谷氨酸受体的刺激诱导多功能激酶p90rsk快速依赖蛋白激酶C的易位至多核糖体；同时，至少六种多核糖体结合蛋白的磷酸化增强。多核糖体结合蛋白中有p90rsk激活激酶ERK-2和一种已知的p90rsk底物糖原合酶激酶3β，其通过真核起始因子2B调节翻译效率。因此，促代谢型谷氨酸受体刺激可通过p90rsk易位至核糖体诱导突触活性依赖性翻译。
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