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首页> 外文期刊>Biochemistry >Activity-Dependent phosphorylation of dynamin 1 at serine 857
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Activity-Dependent phosphorylation of dynamin 1 at serine 857

机译：丝氨酸857上的dynamin 1的活性依赖磷酸化。

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摘要

Dynamin 1 is thought to mediate synaptic transmission through interactions with multiple endocytic accessory proteins in a phosphorylation-dependent manner. Previously, we have shown that DYRK1A, a chromosome 21-encoded kinase implicated in the mental retardation of Down syndrome, phosphorylates primarily serine 857 (S857) in the proline-rich domain, found only in 1xa, one of the alternative C-terminal splicing isoforms of dynamin 1. Dynamin 1xa and 1xb isoforms are able to assemble into heterologous complexes and are coregulated by DYRK1A phosphorylation in binding to amphiphysin in vitro. To help in assessing the physiological significance of S857 phosphorylation, we developed a semiquantitative method for measuring the cellular level of phospho-S857 (pS857). Dynamin 1xa is highly phosphorylated at S857 in resting hippocampal neurons and in a hippocampal cell line, with >60% of all endogenous protein phosphorylated at this residue. In the hippocampus, the level of pS857 is dynamically controlled by synaptic stimulations with the involvement of Ca2+/calcineurin and AMPA/kainate receptors. Immunofluorescence staining shows that pS857 is found in the soma and throughout the entire length of apical dendrites in resting pyramidal neurons. Neuronal stimulation in the Schaffer collateral pathway promotes pS857 dephosphorylation in distal areas of apical dendrites, the region forming synapses with the impinging axons of Schaffer collateral. In summary, our results support the conclusion that S857 phosphorylation is a physiological event and its level is modulated by neuronal activity in nerve terminals.
机译：认为动力蛋白1通过与多个内吞辅助蛋白以磷酸化依赖性方式相互作用来介导突触传递。以前，我们已经证明DYRK1A是21号染色体编码的激酶，与唐氏综合症的智力障碍有关，主要在富含脯氨酸的结构域中磷酸化丝氨酸857（S857），仅在1xa中发现，这是另一种C端剪接动力蛋白的同工型1.动力蛋白1xa和1xb的同工型能够组装成异源复合物，并通过DYRK1A磷酸化在体外与两亲性结合而形成核心。为了帮助评估S857磷酸化的生理意义，我们开发了一种用于测量磷酸S857（pS857）细胞水平的半定量方法。在静止的海马神经元和海马细胞系中，Dynamin 1xa在S857处高度磷酸化，所有内源蛋白的60％以上都在该残基处被磷酸化。在海马中，pS857的水平是由突触刺激动态控制的，其中涉及Ca2 + /钙调神经磷酸酶和AMPA /海藻酸酯受体。免疫荧光染色显示，pS857在体细胞中以及在静止的锥体神经元的整个顶端树突的整个长度中均被发现。 Schaffer侧支通路中的神经元刺激在顶端树突的远端区域促进pS857的去磷酸化，该区域与撞击的Schaffer侧支轴突形成突触。总之，我们的结果支持以下结论：S857磷酸化是一种生理事件，其水平受神经末梢神经元活动的调节。

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