Modelling complexity and redundancy in actin polymerization

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)是一个精确的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招募。这在很大程度上依赖于多聚脯氨酸序列和SH3结合域之间的相互作用。在分子水平上，这看起来像是一个混乱的系统，有多个串联重复和许多相互竞争的相互作用。LAS-17有6个多脯氨酸重复序列，与SLA1(3个SH3)、肌动蛋白(每个单体一个多脯氨酸结合位点)和大约10个其他含有SH3的蛋白质相互作用。有许多互动的亲和力数据。

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.