PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2 protein.

PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2 protein.
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PKC 调节 delta2 谷氨酸受体与 S-SCAM/MAGI-2 蛋白的相互作用。

DOI:
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发表时间:
2003
影响因子:
3.1
通讯作者:
R. Yano
R. Yano
中科院分区:
生物学4区
文献类型:
--
作者:
C. Yap;Y. Muto;H. Kishida;T. Hashikawa;R. Yano

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在细胞内,膜蛋白定位于特定的表面结构域以执行其精确的功能。各种PDZ结构域蛋白已被证明在膜蛋白的细胞内运输和锚定中发挥重要作用。在这项研究中,我们表明,delta 2谷氨酸受体与S-SCAM/MAGI-2,一个PDZ域蛋白定位在小脑浦肯野细胞的核周区和突触后部位的相互作用。结合受PKC(蛋白激酶-C)介导的S-SCAM/MAGI-2中具有独特重复结构的受体的磷酸化调节。这两种蛋白的共表达导致COS 7细胞中受体定位的急剧变化。这些结果显示了PDZ结构域蛋白结合的一种新的调节机制,并表明delta 2受体和S-SCAM/MAGI-2之间的相互作用可能对受体的细胞内运输很重要。
Inside cells, membrane proteins are localized at particular surface domains to perform their precise functions. Various kinds of PDZ domain proteins have been shown to play important roles in the intracellular trafficking and anchoring of membrane proteins. In this study, we show that delta2 glutamate receptor is interacting with S-SCAM/MAGI-2, a PDZ domain protein localized in the perinuclear region and postsynaptic sites of cerebellar Purkinje cells. The binding is regulated by PKC (protein kinase-C) mediated phosphorylation of the receptor with a unique repetitive structure in S-SCAM/MAGI-2. Co-expression of both proteins resulted in drastic changes of the receptor localization in COS7 cells. These results show a novel regulatory mechanism for the binding of PDZ domain proteins and suggest that the interaction between delta2 receptor and S-SCAM/MAGI-2 may be important for intracellular trafficking of the receptor.