Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities
Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities
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DOI：
10.1016/j.febslet.2004.12.009
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发表时间：
2005-01-17
期刊：
影响因子：
3.5
通讯作者：
Fackler, OT
中科院分区：
文献类型：
--
作者：
Madrid, R;Gasteier, JE;Fackler, OT
透明相关的Forin同源2结构域包含蛋白1(FHOD1)与Rac GTP酶相互作用，激活Rho-Rock级联反应，导致肌动蛋白应激纤维的形成。在这里，我们报道了在酵母双杂交系统中，通过免疫共沉淀和哺乳动物细胞中的共定位来检测FHOD1的同型相互作用。预测的卷曲基序C-末端到核心FH2结构域，而不是核心FH2结构域本身，是FHOD1自结合的关键。螺旋卷曲基序和核心FH2结构域的缺失都抑制了FHOD1对肌动蛋白应激纤维的形成和血清反应元件转录的激活。相反，这些基序对于FHOD1与rac1的物理和功能相互作用是必不可少的。综上所述，这些结果表明，FHOD1通过盘绕螺旋基序的齐聚是其生物活性的关键参数。(C)2004年欧洲生化学会联合会。爱思唯尔出版，版权所有。
The diaphanous-related formin homology 2 domain containing protein 1 (FHOD1) interacts with the Rac GTPase and activates the Rho-ROCK cascade leading to the formation of actin stress fibers. Here, we report the detection of homotypic interactions of FHOD1 in the yeast two-hybrid system, by co-immunoprecipitation and co-localization in mammalian cells. A predicted coiled-coil motif C-terminal to the core FH2 domain, but not the core FH2 domain itself, was critical for self-association of FHOD1. Deletion of both the coiled-coil motif and the core FH2 domain abrogated formation of actin stress fibers and activation of transcription of the serum response element by FHOD1. In contrast, these motifs were dispensable for the physical and functional interaction of FHOD1 with Rac1. Together, these results indicate that oligomerization of FHOD1 via the coiled-coil motif is a critical parameter for its biological activities. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.