Mechanics of Z-disc Proteins

Z 盘蛋白的力学

• 批准号: 175309880
• 负责人: Professor Dr. Matthias Rief
• 金额: --
• 依托单位: Lehrstuhl für Molekulare Biophysik
• 依托单位国家: 德国
• 项目类别: Research Units
• 财政年份: 2010
• 资助国家: 德国
• 起止时间: 2009-12-31 至 2017-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/175309880?language=en
• 关键词: Mechanics; disc; Proteins

The muscle Z-disc is a cellular structure constantly subject to considerable mechanical stress. How the molecular structures of the Z-disc are adapted to the forces acting in muscle is largely unkown. In this project we will investigate the mechanical stability of important molecular structures and protein/protein interactions in the muscle Z-disc on the single molecule level. In the first part of the project, we will study the interaction mechanics of filamin. Both the mechanical stability of the dimer as well as the interaction with multiple binding partners will be investigated. The second area will concern the interaction mechanics of the calmodulin like domains in α-actinin. The interaction of this domain with the titin Zrepeats is a key anchoring mechanism of titin within the Z-disc.

肌肉Z盘是一种不断受到相当大的机械应力的细胞结构。Z盘的分子结构如何适应肌肉中的作用力在很大程度上是未知的。在这个项目中，我们将在单分子水平上研究肌肉Z盘中重要分子结构和蛋白质/蛋白质相互作用的机械稳定性。在本项目的第一部分，我们将研究细丝蛋白的相互作用机制。将研究二聚体的机械稳定性以及与多个结合伴侣的相互作用。第二个方面是α-辅肌动蛋白中钙调素样结构域的相互作用机制。该结构域与肌联蛋白Z重复序列的相互作用是肌联蛋白在Z盘内的关键锚定机制。

项目成果

Force-dependent isomerization kinetics of a highly conserved proline switch modulates the mechanosensing region of filamin

• DOI: 10.1073/pnas.1319448111
• 发表时间: 2014-04-15
• 期刊: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• 影响因子: 11.1
• 作者: Rognoni, Lorenz;Moest, Tobias;Rief, Matthias
• 通讯作者: Rief, Matthias

Dynamic force sensing of filamin revealed in single-molecule experiments

• DOI: 10.1073/pnas.1211274109
• 发表时间: 2012-11-27
• 期刊: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• 影响因子: 11.1
• 作者: Rognoni, Lorenz;Stigler, Johannes;Rief, Matthias
• 通讯作者: Rief, Matthias