To characterize how protein-protein interaction (PPI) networks change, we quantified the relative PPI abundance of 1.6 million protein pairs in yeast across 9 growth conditions, with replication, for a total of 44 million measurements. Our multi-condition screen identified 13,764 pairwise PPIs, a 3-fold increase over PPIs identified in one condition. A few immutable PPIs are present across all conditions, while most mutable PPIs are rarely observed. Immutable PPIs aggregate into highly connected core network modules, with most network remodeling occurring within a loosely connected accessory module. Mutable PPIs are less likely to co-express, co-localize, and be explained by simple mass action kinetics, and more likely to contain proteins with intrinsically disordered regions, implying that environment-dependent association and binding is critical to cellular adaptation. Our results show that protein interactomes are larger than previously thought and contain highly dynamic regions that reorganize to drive or respond to cellular changes.

中文翻译：

---

大型辅助蛋白相互作用组跨环境重新连接

为了表征蛋白质-蛋白质相互作用（PPI）网络如何变化，我们量化了9种生长条件下酵母中160万蛋白质对的相对PPI丰度，并进行了复制，总共进行了4400万次测量。我们的多条件筛选可识别出13,764个成对的PPI，比一种情况下识别的PPI增长了3倍。在所有条件下都存在一些不变的PPI，而很少观察到大多数可变的PPI。不可变的PPI聚集到高度连接的核心网络模块中，大多数网络重构发生在松散连接的附件模块中。可变的PPI不太可能共表达，共定位并通过简单的质量动力学来解释，而更有可能包含具有内在无序区域的蛋白质，这意味着依赖于环境的关联和结合对于细胞适应至关重要。我们的结果表明，蛋白质相互作用组比以前认为的要大，并且包含高度动态的区域，这些区域会重组以驱动或响应细胞变化。