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首页> 外文期刊>Genes to cells : >Keratin-binding ability of the N-terminal Solo domain of Solo is critical for its function in cellular mechanotransduction
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Keratin-binding ability of the N-terminal Solo domain of Solo is critical for its function in cellular mechanotransduction

机译：单末端单位域的角蛋白结合能力对于其在细胞机械调节中的功能至关重要

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摘要

Solo (ARHGEF40) is a RhoA-targeting guanine nucleotide exchange factor that regulates tensional force-induced cytoskeletal reorganization. Solo binds to keratin 8/keratin 18 (K8/K18) filaments through multiple sites, but the roles of these interactions in the localization and mechanotransduction-regulating function of Solo remain unclear. Here, we constructed two Solo mutants (L14R/L17R and L49R/L52R) with leucine-to-arginine replacements in the N-terminal conserved region (which we termed the Solo domain) and analyzed their K18-binding activities. These mutations markedly decreased the K18-binding ability of the N-terminal fragment (residues 1-329) of Solo but had no apparent effect on the K18-binding ability of full-length (FL) Solo. When expressed in cultured cells, wild-type Solo-FL showed a unique punctate localization near the ventral surface of cells and caused the reinforcement of actin filaments. In contrast, despite retaining the K18-binding ability, the L14R/L17R and L49R/L52R mutants of Solo-FL were diffusely distributed in the cytoplasm and barely induced actin cytoskeletal reinforcement. Furthermore, wild-type Solo-FL promoted traction force generation against extracellular matrices and tensional force-induced stress fiber reinforcement, but its L14R/L17R and L49R/L52R mutants did not. These results suggest that the K18-binding ability of the N-terminal Solo domain is critical for the ventral localization of Solo and its function in regulating mechanotransduction.
机译：Solo（Arhgef40）是诱导鸟嘌呤核苷酸交换因子，调节张力诱导的细胞骨骼重组。通过多个位点与角蛋白8 /角蛋白18（K8 / K18）长丝结合，但这些相互作用在局部化和机械调节函数中的作用仍不清楚。这里，我们在N末端保守区（我们称为SOLO结构域的亮氨酸 - 精氨酸替换并分析了它们的K18结合活性，构建了两种唯一突变体（L14R / L17R和L52R）。这些突变显着降低了Solo的N-末端片段（残基1-329）的K18结合能力，但对全长（FL）唯一的K18结合能力没有明显影响。当在培养细胞中表达时，野生型Solo-FL在细胞的腹表面附近显示出独特的点状定位，并导致肌动蛋白长丝的增强。相反，尽管保持了K18结合能力，但Solo-Fl的L14R / L17R和L49R / L52R突变体在细胞质中弥漫性分布，并仅诱导肌动蛋白细胞骨骼增强件。此外，野生型Solo-FL促进牵引力产生针对细胞外基质的牵引力和张力诱导的应力纤维增强，但其L14R / L17R和L49R / L52R突变体没有。这些结果表明，N-末端SOLO结构域的K18结合能力对于Solo的腹侧定位至关重要，其在调节机电站中的功能。

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