丝裂原活化蛋白激酶（MAPK）对接位点在树突状mRNA运输中对Staufen2蛋白的作用。

Role of mitogen-activated protein kinase (MAPK) docking sites on Staufen2 protein in dendritic mRNA transport.

作者信息

Nam Yeon-Ju, Cheon Hyo-Soon, Choi Young-Ki, Kim Seok-Yong, Shin Eun-Young, Kim Eung-Gook, Kim Hyong Kyu

机构信息

Department of Medicine and Microbiology, College of Medicine, Signaling Disorder Research Center, Chungbuk National University, Sungbong-ro 410, Cheongju 361-763, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2008 Aug 8;372(4):525-9. doi: 10.1016/j.bbrc.2008.05.047. Epub 2008 May 19.

DOI:10.1016/j.bbrc.2008.05.047

Abstract

Although transport and subsequent translation of dendritic mRNA play an important role in neuronal synaptic plasticity, the underlying mechanisms for modulating dendritic mRNA transport are almost completely unknown. In this study, we identified and characterized an interaction between Staufen2 and mitogen-activated protein kinase (MAPK) with co-immunoprecipitation assays. Staufen2 utilized a docking (D) site to interact with ERK1/2; deleting the D-site decreased colocalization of Staufen2 with immunoreactive ERK1/2 in the cell body regions of cultured hippocampal neurons, and it reduced the amount of Staufen2-containing RNP complexes in the distal dendrites. In addition, the deletion completely abolished the depolarization-induced increase of Staufen2-containing RNP complexes. These results suggest that the MAPK pathway could modulate dendritic mRNA transport through its interaction with Staufen2.

摘要

尽管树突状mRNA的运输及随后的翻译在神经元突触可塑性中发挥着重要作用，但调节树突状mRNA运输的潜在机制几乎完全未知。在本研究中，我们通过免疫共沉淀实验鉴定并表征了Staufen2与丝裂原活化蛋白激酶（MAPK）之间的相互作用。Staufen2利用一个对接（D）位点与ERK1/2相互作用；删除该D位点会减少培养的海马神经元细胞体区域中Staufen2与免疫反应性ERK1/2的共定位，并减少远端树突中含Staufen2的核糖核蛋白复合物的数量。此外，该缺失完全消除了去极化诱导的含Staufen2的核糖核蛋白复合物的增加。这些结果表明，MAPK通路可通过与Staufen2的相互作用来调节树突状mRNA的运输。