Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling
Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling
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DOI：
10.1126/science.284.5417.1161
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发表时间：
1999-05-14
期刊：
影响因子：
56.9
通讯作者：
Snyder, SH
中科院分区：
文献类型：
--
作者：
Sabatini, DM;Barrow, RK;Snyder, SH
RAFT 1（雷帕霉素和FKBP 12靶标1;也称为FRAP或mTOR）是ATM（共济失调毛细血管扩张突变）相关蛋白家族的成员，并作为免疫抑制剂雷帕霉素作用的体内介体和信使RNA翻译的重要调节剂发挥作用。在哺乳动物细胞中，RAFT 1与桥蛋白相互作用，桥蛋白是一种广泛表达的蛋白质，是神经元细胞膜上甘氨酸受体聚集所必需的。不能与桥蛋白结合的RAFT 1突变体不能向下游分子发出信号，包括p70核糖体56激酶和eIF-4 E结合蛋白4 E-BP 1。与gephyrin的相互作用归因于ATM相关蛋白的大氨基末端区域的功能，并揭示了聚类蛋白gephyrin在信号转导中的作用。
RAFT1 (rapamycin and FKBP12 target 1; also called FRAP or mTOR) is a member of the ATM (ataxia telangiectasia mutated)-related family of proteins and functions as the in vivo mediator of the effects of the immunosuppressant rapamycin and as an important regulator of messenger RNA translation. In mammalian cells RAFT1 interacted with gephyrin, a widely expressed protein necessary for the clustering of glycine receptors at the cell membrane of neurons. RAFT1 mutants that could not associate with gephyrin failed to signal to downstream molecules, including the p70 ribosomal 56 kinase and the eIF-4E binding protein, 4E-BP1. The interaction with gephyrin ascribes a function to the Large amino-terminal region of an ATM-related protein and reveals a role in signal transduction for the clustering protein gephyrin.