Modelling complexity and redundancy in actin polymerization

肌动蛋白聚合的复杂性和冗余建模

• 批准号: 2109100
• 金额: --
• 依托单位: University of Sheffield
• 依托单位国家: 英国
• 项目类别: Studentship
• 财政年份: 2018
• 资助国家: 英国
• 起止时间: 2018 至 无数据
• 项目状态: 已结题
• 来源: https://gtr.ukri.org/projects?ref=studentship-2109100
• 关键词: Modelling; complexity; redundancy; actin; polymerization

The Ayscough lab has shown that actin polymerization in yeast (for example during endocytosis) is a precisely timed and orchestrated event, with different proteins recruited at predictable times and orders. Much of it relies on interactions between polyproline sequences and SH3 binding domains. At a molecular level this looks like a messy system, with multiple tandem repeats and many competing interactions. Las-17 has 6 polyproline repeats and interacts with SLA1 (3 SH3), actin (one polyproline binding site per monomer) and about 10 other SH3-containing proteins. There is affinity data for many of the interactions.

Ayscough实验室已经证明，酵母中的肌动蛋白聚合（例如在内吞过程中）是一个精确定时和精心安排的事件，不同的蛋白质在可预测的时间和顺序被招募。它很大程度上依赖于脯氨酸序列和SH3结合域之间的相互作用。在分子水平上，这看起来像一个混乱的系统，有多个串联重复和许多相互竞争的相互作用。Las-17有6个脯氨酸重复序列，与SLA1（3个SH3）、肌动蛋白（每个单体一个脯氨酸结合位点）和约10个其他含SH3的蛋白相互作用。有许多相互作用的亲和性数据。