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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Phosphorylation of spinophilin by ERK and cyclin-dependent PK 5 (Cdk5)
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Phosphorylation of spinophilin by ERK and cyclin-dependent PK 5 (Cdk5)

机译：ERK和依赖细胞周期蛋白的PK 5（Cdk5）使亲脂蛋白磷酸化

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摘要

Spinophilin is a protein that binds to protein phosphatase-1 and actin and modulates excitatory synaptic transmission and dendritic spine morphology. We have identified three sites phosphorylated by ERK2 (Ser-15 and Ser-205) and cyclin-dependent PK 5 (Cdk5) (Ser-17), within the actin-binding domain of spinophilin. Cdk5 and ERK2 both phosphorylated spinophilin in intact cells. However, in vitro, phosphorylation by ERK2, but not by Cdk5, was able to modulate the ability of spinophilin to bind to and bundle actin filaments. In neurons and HEK293 cells expressing GFP-tagged variants of spinophilin, imaging studies demonstrated that introduction of a phospho-site mimic (Ser-15 to glutamate) was associated with increased filopodial density. These results support a role for spinophilin phosphorylation by ERK2 in the regulation of spine morphogenesis.
机译：Spinophilin是一种与磷酸酶1和肌动蛋白结合的蛋白，可调节兴奋性突触传递和树突棘形态。我们已经确定了在亲脂蛋白的肌动蛋白结合域内被ERK2（Ser-15和Ser-205）和细胞周期蛋白依赖性PK 5（Cdk5）（Ser-17）磷酸化的三个位点。 Cdk5和ERK2都在完整细胞中磷酸化了亲脂蛋白。但是，在体外，ERK2而不是Cdk5的磷酸化能够调节亲旋蛋白结合并束缚肌动蛋白丝的能力。在表达GFP标记的亲丝蛋白变体的神经元和HEK293细胞中，影像学研究表明，引入磷酸位点模拟物（谷氨酸的Ser-15）与增加的丝虫密度有关。这些结果支持ERK2的亲脂蛋白磷酸化在调节脊柱形态发生中的作用。

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