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首页> 外文期刊>Neuroscience Letters: An International Multidisciplinary Journal Devoted to the Rapid Publication of Basic Research in the Brain Sciences >Site-specific phosphorylation of SCG10 in neuronal plasticity: role of Ser73 phosphorylation by N-methyl D-aspartic acid receptor activation in rat hippocampus.
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Site-specific phosphorylation of SCG10 in neuronal plasticity: role of Ser73 phosphorylation by N-methyl D-aspartic acid receptor activation in rat hippocampus.

机译：SCG10在神经元可塑性中的位点特异性磷酸化：大鼠海马中N-甲基D-天冬氨酸受体激活引起的Ser73磷酸化作用。

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Accumulated evidence suggests that actin and microtubule regulating proteins contribute to neuronal structural dynamics, which subsequently affect neuronal plasticity. SCG10 is a neuronal-specific stathmin protein with microtubule destabilizing activity that is affected by multiple phosphorylation, at least in vitro. SCG10 has four major phosphorylation sites: Ser50 and Ser97 targeted by protein kinase A (PKA), and Ser62 and Ser73 targeted by mitogen-activated protein kinase (MAPK). To explore the potential roles of site-specific phosphorylation in physiological models, we developed phosphorylation site-specific antibodies and examined the SCG10 status in primary cultured hippocampal neurons and tissues. Although SCG10 is concentrated in growth cones and the Golgi apparatus in primary cultured neurons, the phosphorylated form was also detected in both regions, suggesting that MT dynamics within the growth cone may be regulated by protein phosphorylation. In the adult hippocampus, an intense stimulus such as kainate treatment induced a rapid phosphorylation of Ser73 within 15 min that was sustained for at least 60 min. This response was mediated through the N-methyl D-aspartic acid (NMDA) receptor and was ablated by the antagonist MK-801. The MAPK enzyme Erk2 was simultaneously activated along a similar time course to SCG10, suggesting that Erk2 may directly phosphorylate Ser73. These results demonstrate that changes in the phosphorylation status of SCG10 in vivo, dependent upon neural activity and/or plasticity, could affect the microtubule dynamics in neuronal dendrites.
机译：积累的证据表明肌动蛋白和微管调节蛋白有助于神经元结构动力学，从而影响神经元可塑性。 SCG10是具有微管去稳定活性的神经元特定的athathmin蛋白，至少在体外受多重磷酸化影响。 SCG10具有四个主要的磷酸化位点：被蛋白激酶A（PKA）靶向的Ser50和Ser97，以及被促分裂原激活蛋白激酶（MAPK）靶向的Ser62和Ser73。为了探索位点特异性磷酸化在生理模型中的潜在作用，我们开发了位点特异性磷酸化抗体，并检查了原代培养的海马神经元和组织中SCG10的状态。尽管SCG10集中在生长锥中，而高尔基体集中在原代培养的神经元中，但在两个区域中也都检测到了磷酸化形式，这表明生长锥内的MT动态可能受蛋白质磷酸化的调节。在成年海马中，强烈的刺激（如海藻酸盐治疗）可在15分钟内诱导Ser73迅速磷酸化，并持续至少60分钟。该反应通过N-甲基D-天冬氨酸（NMDA）受体介导，并被拮抗剂MK-801消除。 MAPK酶Erk2在与SCG10相似的时间过程中同时被激活，表明Erk2可能直接磷酸化Ser73。这些结果表明，取决于神经活动和/或可塑性，SCG10体内磷酸化状态的改变可能会影响神经元树突中的微管动力学。

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