Association of membrane-associated guanylate kinase-interacting protein-1 with Raf-1
Association of membrane-associated guanylate kinase-interacting protein-1 with Raf-1
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DOI：
10.1006/bbrc.2000.2475
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发表时间：
2000-04-13
影响因子：
3.1
通讯作者：
Hata, Y
中科院分区：
文献类型：
--
作者：
Yao, I;Ohtsuka, T;Hata, Y
膜相关鸟苷酸激酶相互作用蛋白 (MAGUIN)-1 被鉴定为与突触支架分子 (S-SCAM) 和突触后密度 (PSD)-95/突触相关蛋白 (SAP)SO 相互作用的蛋白质。 MAGUIN-1 具有由一个不育α蛾、一个 PSD-95/Dlg-A/ZO-1 (PDZ) 和一个 pleckstrin 同源 (PH) 结构域组成的嵌合分子结构，并通过其羧基末端 PDZ 结合基序与 S SCAM 和 PSD-95/SAP90 的 PDZ 结构域相互作用。 MAGUIN-1 被认为是果蝇 CNK 的哺乳动物同源物，果蝇 CNK 是一种与眼睛发育调节有关的 Raf 相互作用蛋白。在这里我们测试了 MAGUIN-1 是否直接与 Raf-l 相互作用。 MAGUIN-1和Raf-1是共免疫沉淀的大鼠大脑。 MAGUIN-1与Raf-1的激酶结构域结合，并且Raf-1与含有PH结构域的MAGUIN-1的中部区域结合。然而，与Ki-Ras的显性活性突变体相比，Ki-Ras与Raf-1相互作用，将其从胞质溶胶募集至质膜并激活它，MAGUIN-1既不激活Raf-1也不将其募集至质膜。 MAGUIN-1可能将Raf-1与PSD-95/SAP90和S-SCAM组装的突触组件连接起来。 (C) 2000 年学术出版社。
Membrane-associated guanylate kinase-interacting protein (MAGUIN)-1 was identified as a protein interacting with synaptic scaffolding molecule (S-SCAM) and postsynaptic density (PSD)-95/synapse-associated protein (SAP)SO. MAGUIN-1 has a chimerical molecular structure composed of one sterile alpha moth, one PSD-95/Dlg-A/ZO-1 (PDZ), and one pleckstrin homology (PH) domain, and interacts with the PDZ domains of S SCAM and PSD-95/SAP90 via its carboxyl-terminal PDZ-binding motif. MAGUIN-1 is considered as a mammalian homologue of Drosophila CNK which is a Raf-interacting protein implicated in the regulation of eye development. Here we have tested whether MAGUIN-1 interacts directly with Raf-l. MAGUIN-1 and Raf-l were coimmunoprecipitated hem rat brain. MAGUIN-1 binds to the kinase domain of Raf-l, and Raf-l binds to the mid die region of MAGUIN-1 containing the PH domain. However, in contrast to the dominant active mutant of Ki-Ras, which interacts with Raf-l, recruits it to the plasma membrane from the cytosol, and activates it, MAGUIN-1 neither activates Raf-l nor recruits it to the plasma membrane. MAGUIN-1 may link Raf-l to components of synapses assembled by PSD-95/SAP90 and S-SCAM. (C) 2000 Academic Press.