When the small ribosomal subunit binds to mRNA’s 5’-cap, it looks for the complex of three eLFs bound to the poly-A-binding protein (PABP), which circularises the mRNA. It is then this circular mRNA that the small ribosomal subunit binds to.

In low-nutrient environments, 4E-BP1 binds to PABP, inhibiting it from binding to the 5’-cap complex. I high nutrient environments 4E-BP1 is phosphorylated.

Why (what benefit is conferred?) are the eLFs there? Why not just have the PABP bind to the 5’-cap to initiate transcription? And why 4E-BP1? Why not just phosphorylate PABP directly?
I mean I know that as is, PABP isn’t set up to be usefully phosphorylated, but why is it this way? It seems a whole bunch energy and resources wasted making these extra proteins, and more room for things to go wrong, more DNA that has to be made and carried around with no mutations and transcribed and translated correctly.