Centre for High-Throughput Biology, University of British Columbia, East Mall, Vancouver V6T 1Z4, Canada.
Biochem J. 2013 Sep 15;454(3):361-9. doi: 10.1042/BJ20130545.
Because of their pervasiveness in eukaryotic genomes and their unique properties, understanding the role that ID (intrinsically disordered) regions in proteins play in the interactome is essential for gaining a better understanding of the network. Especially critical in determining this role is their ability to bind more than one partner using the same region. Studies have revealed that proteins containing ID regions tend to take a central role in protein interaction networks; specifically, they act as hubs, interacting with multiple different partners across time and space, allowing for the co-ordination of many cellular activities. There appear to be three different modules within ID regions responsible for their functionally promiscuous behaviour: MoRFs (molecular recognition features), SLiMs (small linear motifs) and LCRs (low complexity regions). These regions allow for functionality such as engaging in the formation of dynamic heteromeric structures which can serve to increase local activity of an enzyme or store a collection of functionally related molecules for later use. However, the use of promiscuity does not come without a cost: a number of diseases that have been associated with ID-containing proteins seem to be caused by undesirable interactions occurring upon altered expression of the ID-containing protein.
由于它们在真核生物基因组中的普遍性及其独特的性质，了解蛋白质中 ID（无序）区域在互作组中的作用对于更好地理解网络是至关重要的。特别关键的是它们能够使用同一区域结合多个伴侣的能力。研究表明，含有 ID 区域的蛋白质往往在蛋白质相互作用网络中发挥核心作用；具体来说，它们充当枢纽，在时间和空间上与多个不同的伴侣相互作用，从而协调许多细胞活动。ID 区域内似乎有三个不同的模块负责其功能上的混杂行为：MoRFs（分子识别特征）、SLiMs（小线性基序）和 LCRs（低复杂度区域）。这些区域允许进行功能，如参与形成动态异源结构，这可以增加酶的局部活性或储存一组功能相关的分子以备后用。然而，混杂性的使用并非没有代价：一些与含有 ID 的蛋白质相关的疾病似乎是由于 ID 含有蛋白质的异常表达导致的不期望的相互作用引起的。
