RNA-Binding Proteins (RBPs) are dynamic assemblages between mRNAs and different proteins that form messenger ribonucleoprotein complexes (mRNPs). These complexes are essential for the regulation of gene expression to ensure that all the steps are performed correctly throughout the whole process. Therefore, they are important control factors for protein levels and cell phenotypes. Moreover, they affect mRNA stability by regulating its conformation due to the environment, stress or extracellular signals. However, their ability to bind and control such a wide variety of RNA targets allows them to form complex regulatory networks (PTRNs).These networks represent a challenge to study each RNA-binding protein individually.  Thankfully, due to new methodological advances, the identification of RBPs is slowly expanding, which demonstrates that they are contained in broad families of proteins. RBPs can significantly impact multiple biological processes, and have to be very accurately expressed. Overexpression can change the mRNA target rate, binding to low-affinity RNA sites and causing deleterious results on cellular fitness. Not being able to synthesize at the right level is also problematic because it can lead to cell death. Therefore, RBPs are regulated via auto-regulation, so they are in control of their own actions. Furthermore, they use both negative feedback, to maintain homeostasis, and positive feedback, to create binary genetic changes in the cell.
In metazoans and bacteria, many genes involved in post-post transcriptional regulation are regulated post transcriptionally. For Drosophila RBPs associated with splicing or nonsense mediated decay, analyses of protein-protein and protein-RNA interaction profiles have revealed ubiquitous interactions with RNA and protein products of the same gene. It remains unclear whether these observations are driven by ribosome proximal or ribosome mediated contacts, or if some protein complexes, particularly RNPs, undergo co-translational assembly.