Synaptic stimulation alters protein phosphorylation in vivo in a single Aplysia neuron.
Synaptic stimulation alters protein phosphorylation in vivo in a single Aplysia neuron.
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突触刺激改变单个海兔神经元体内的蛋白质磷酸化。
DOI：
10.1073/pnas.81.10.3233
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发表时间：
1984
影响因子：
11.1
通讯作者：
I. Levitan
中科院分区：
文献类型：
--
作者：
J. Lemos;I. Novak‐Hofer;I. Levitan
在体内，在胞内注射[γ-（32）P]ATP后，在鉴定的失智症神经元R15中检查蛋白磷酸化。二维凝胶电泳分析表明，至少有70个蛋白质磷酸化的R15在50分钟的标记期间。5-羟色胺（5-HT）的应用导致R15中K（+）电导的增加和磷酸化模式的伴随变化：某些蛋白质的磷酸化增加或减少，并且至少出现了5种在对照细胞中未观察到的磷酸化蛋白。多巴胺导致R15的电压依赖性内向电导降低，也改变了磷酸化模式：一些磷酸化变化与5 HT产生的变化相似，而另一些则是多巴胺独有的。刺激通向腹神经节的鳃神经导致R15的持久突触超极化。这种反应背后的电导变化包括K（+）电导的增加（与5 HT产生的电导相同）以及电压依赖性内向电导的减少（与多巴胺产生的电导相同）。刺激鳃神经引起的R15磷酸化变化类似于5-HT和多巴胺引起的变化的组合。结果表明，突触刺激可以调节单个突触后神经元中特定蛋白的磷酸化，并且与蛋白磷酸化可以调节神经元离子通道活性的假设一致。
Protein phosphorylation was examined in the identified Aplysia neuron R15, in vivo, after the intracellular injection of [gamma-(32)P]ATP. Two-dimensional gel electrophoretic analysis indicates that at least 70 proteins are phosphorylated within R15 during a 50-min labeling period. Application of serotonin (5HT) results in an increase in K(+) conductance in R15 and a concomitant change in the phosphorylation pattern: there are increases or decreases in the phosphorylation of some proteins, and at least five phosphoproteins appear that are not observed in control cells. Dopamine causes a decrease in voltage-dependent inward conductance in R15 and also alters the phosphorylation pattern: several of the phosphorylation changes are similar to those produced by 5HT, while others are unique to dopamine. Stimulation of the branchial nerve leading to the abdominal ganglion results in a long-lasting synaptic hyperpolarization of R15. The conductance changes underlying this response include an increase in K(+) conductance (identical to that produced by 5HT) together with a decrease in voltage-dependent inward conductance (identical to that produced by dopamine). The phosphorylation changes induced in R15 by branchial nerve stimulation resemble a combination of the changes induced by 5HT and dopamine. The results demonstrate that synaptic stimulation can modulate the phosphorylation of specific proteins in a single identified postsynaptic neuron and are consistent with the hypothesis that protein phosphorylation can regulate the regulate the activity of neuronal ion channels.