mRNA metabolism is tightly orchestrated by highly-regulated RNA Binding Proteins 
(RBPs) that determine mRNA fate, thereby influencing multiple cellular functions 
across biological contexts. Here, we review the interplay between six well-known 
RBPs (TTP, AUF-1, KSRP, HuR, TIA-1, and TIAR) that recognize AU-rich elements 
(AREs) at the 3' untranslated regions of mRNAs, namely ARE-RBPs. Examples of the 
links between their cross-regulations and modulation of their targets are 
analyzed during mRNA processing, turnover, localization, and translational 
control. Furthermore, ARE recognition can be self-regulated by several factors 
that lead to the prevalence of one RBP over another. Consequently, we examine 
the factors that modulate the dynamics of those protein-RNA transient 
interactions to better understand the final consequences of the regulation 
mediated by ARE-RBPs. For instance, factors controlling the RBP isoforms, their 
conformational state or their post-translational modifications (PTMs) can 
strongly determine the fate of the protein-RNA complexes. Moreover, mRNA 
specific sequence and secondary structure or subtle environmental changes are 
also key determinants to take into account. To sum up, the whole understanding 
of such a fine tuned regulation is a challenge for future research and requires 
the integration of all the available structural and functional data by in vivo, 
in vitro and in silico approaches.