• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Actin filament bundling and different nucleating effects of mouse Diaphanous-related formin FH2 domains on actin/ADF and actin/cofilin complexes.
【24h】

Actin filament bundling and different nucleating effects of mouse Diaphanous-related formin FH2 domains on actin/ADF and actin/cofilin complexes.

机译：肌动蛋白丝束捆绑和小鼠透辉相关的formin FH2结构域对肌动蛋白/ ADF和肌动蛋白/ cofilin复合物的不同成核作用。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Mouse Diaphanous-related formins (mDias) are members of the formin protein family that nucleate actin polymerization and subsequently promote filamentous actin (F-actin) elongation by monomer addition to fast-growing barbed ends. It has been suggested that mDias preferentially recruit actin complexed to profilin due to their proline-rich FH1 domains. During filament elongation, dimeric mDias remain attached to the barbed ends by their FH2 domains, which form an anti-parallel ring-like structure enclosing the filament barbed ends. Dimer formation of mDia-FH2 domains is dependent on their N-terminal lasso and linker subdomains (connector). Here, we investigated the effect of isolated FH2 domains on actin polymerization using mDia1-FH2 domain plus connector, as well as core mDia1, mDia2, and mDia3 missing the connector, by cosedimentation and electron microscopy after negative staining. Analytical ultracentrifugation showed that core FH2 domains of mDia1 and mDia2 exhibited a low degree of dimer formation, whereas mDia3-FH2 minus connector and mDia1-FH2 plus connector readily dimerized. Only core mDia3-FH2 was able to nucleate actin polymerization. However, all tested core FH2 domains decorated and bundled F-actin, as demonstrated by electron microscopy after negative staining. Bundling activity was highest for mDia3-FH2, decreased for mDia2-FH2, and further decreased for mDia1-FH2. The mDia1-FH2 domain plus connector induced actin polymerization also in the absence of profilin, but failed to induce F-actin deformation and bundling. We also tested whether mDia1-FH2 was able to repolymerize actin in complex with different proteins that stabilize globular actin. The data obtained demonstrated that mDia1-FH2 induced actin repolymerization only from the actin/cofilin-1 complex, but not when complexed to actin depolymerizing factor, gelsolin segment 1, vitamin D binding protein, or deoxyribonuclease I.
机译：小鼠透照相关的formins（mDias）是formin蛋白家族的成员，它使肌动蛋白聚合成核，随后通过向快速增长的带刺末端添加单体来促进丝状肌动蛋白（F-actin）延长。有人提出，由于mDias富含脯氨酸的FH1结构域，它们优先招募与profilin复合的肌动蛋白。在长丝伸长过程中，二聚体mDias通过其FH2域保持与带刺的末端相连，该FH2结构域形成包围长丝带刺末端的反平行环状结构。 mDia-FH2结构域的二聚体形成取决于其N末端套索和接头子结构域（连接子）。在这里，我们通过消沉染色和电子显微镜观察了分离的FH2域对使用mDia1-FH2域加连接器以及缺少连接器的核心mDia1，mDia2和mDia3的肌动蛋白聚合的影响，其方法是通过负染色后的沉降和电子显微镜观察。分析超速离心显示，mDia1和mDia2的核心FH2结构域显示出较低的二聚体形成程度，而mDia3-FH2减去接头和mDia1-FH2加上接头很容易二聚。只有核心mDia3-FH2能够使肌动蛋白聚合成核。但是，所有测试的核心FH2结构域都修饰并捆绑了F-肌动蛋白，如负染色后的电子显微镜所示。对于mDia3-FH2，捆绑活动最高，对于mDia2-FH2，捆绑活动降低，对于mDia1-FH2，捆绑活动进一步降低。 mDia1-FH2结构域加连接子在没有profilin的情况下也诱导了肌动蛋白聚合，但未能诱导F-肌动蛋白变形和束缚。我们还测试了mDia1-FH2是否能够与稳定球状肌动蛋白的不同蛋白质复合聚合肌动蛋白。获得的数据表明，mDia1-FH2仅从肌动蛋白/ cofilin-1复合物诱导肌动蛋白再聚合，而与肌动蛋白解聚因子，凝溶胶蛋白节段1，维生素D结合蛋白或脱氧核糖核酸酶I结合时则不诱导肌动蛋白再聚合。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号