Lunenfeld Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue R988, Toronto, Ontario M5G 1X50, Canada; Department of Molecular Genetics and Department of Laboratory Medicine and Pathology, Department of Medicine, University of Toronto, Canada.
Trends Biochem Sci. 2015 Nov;40(11):673-686. doi: 10.1016/j.tibs.2015.08.010. Epub 2015 Oct 1.
Our attraction to precision and symmetry in everyday life must be put aside to appreciate how natural selection favors networks governed by weak interactions, multivalency, and proteins described as low complexity (LC) and/or intrinsically disordered (ID). Phosphorylation, ubiquitination, and glycosylation of proteins often act as weak docking sites for multivalent adaptor proteins in the formation of membrane-associated and soluble complexes that mediate information flow in cells. Multiple post-translational modification (PTM) sites together with LC and ID regions in proteins can mediate phase transition from soluble complexes to liquid droplets in the cytoplasm or tethering to the membrane. Although compositionally complex and highly dynamic, these systems display remarkable control of specificity, timing, and switch-like behavior in signaling pathways.
我们日常生活中对精确和对称的追求必须放在一边，以欣赏自然选择如何偏爱由弱相互作用、多价性以及被描述为低复杂度 (LC) 和/或固有无序 (ID) 的蛋白质控制的网络。蛋白质的磷酸化、泛素化和糖基化通常作为多价衔接蛋白的弱结合位点，在形成膜相关和可溶性复合物中发挥作用，这些复合物介导细胞中的信息流。多个翻译后修饰 (PTM) 位点以及蛋白质中的 LC 和 ID 区域可以介导从可溶性复合物到细胞质中的液滴或与膜连接的相变。尽管这些系统在组成上复杂且高度动态，但它们在信号通路中表现出对特异性、时间和类似开关的行为的显著控制。
