Characterization of Rab45/RASEF containing EF-hand domain and a coiled-coil motif as a self-associating GTPase
Characterization of Rab45/RASEF containing EF-hand domain and a coiled-coil motif as a self-associating GTPase
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DOI：
10.1016/j.bbrc.2007.03.206
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发表时间：
2007-06-08
影响因子：
3.1
通讯作者：
Katada, Toshiaki
中科院分区：
文献类型：
--
作者：
Shintani, Mami;Tada, Minoru;Katada, Toshiaki
Rab-family GTP酶作为膜运输的关键调节因子发挥作用。其中Rab 45/RASEF是一种非典型的GTdR，它在中间区域含有卷曲螺旋基序，在N-末端有一个独特的EF-手结构域，C-末端有Rab-homologous结构域。在这里，我们提供了初步的生化特性和细胞内定位的人Rab 45。Rab 45通过C-末端Rab结构域结合鸟嘌呤核苷酸三磷酸和二磷酸。Rab 45具有自我相互作用的能力，而自我相互作用需要含有卷曲螺旋基序的中间区域。Rab 45在HeLa细胞中的表达定位于细胞核周区的小块区域中，并且该定位受Rab 45的鸟嘌呤核苷酸结合状态的调节。有趣的是，中间区域，与Rab结构域，似乎是必不可少的特征性的核周定位的Rab 45，表明自身相互作用可能参与细胞内定位的Rab 45。(c)2007爱思唯尔公司All rights reserved.
Rab-family GTPases function as key regulators for membrane traffic. Among them, Rab45/RASEF is an atypical GTPase in that it contains a coiled-coil motif at the mid region and a distinct N-terminal EF-hand domain with C-terminal Rab-homology domain. Here, we provide the initial biochemical characterization and intracellular localization of human Rab45. Rab45 bound guanine nucleotide tri- and di-phosphates through the C-terminal Rab domain. Rab45 was capable of self-interacting, and the self-interaction required the mid region containing the coiled-coil motif. Rab45 expressed in HeLa cells was localized in a small patch in the perinuclear area of the cell, and the localization was regulated by the guanine nucleotide-bound states of Rab45. Interestingly, the mid region, together with Rab domain, appeared to be essential for the characteristic perinuclear localization of Rab45, indicating that the self-interaction may be involved in the intracellular localization of Rab45. (c) 2007 Elsevier Inc. All rights reserved.