Hu proteins are RNA-binding proteins that bind to adenosine-uridine (AU)-rich elements (AREs). Hu proteins affect almost every posttranscriptional aspect of RNA metabolism, including the control of mRNA translation. HuD is one member of the neuronal Hu family of proteins and promotes neuronal differentiation. We have previously shown that HuD enhances cap-dependent translation through a direct interaction with eIF4A and poly(A). We have also shown that the stimulatory effect of HuD on neurite outgrowth depends on the interaction of HuD with eIF4A- and poly(A). We further explored the underlying molecular interactions and found that RNA-bound HuD directly and specifically interacts with phosphorylated Akt1, and this interaction is required for HuD-induced neurite outgrowth in PC12 cells. Here we show that phosphorylated Akt1 is recruited in a HuD-dependent manner into the cap-binding complex. We also observe that this leads to increased levels of phosphorylated eIF4B within the cap-binding complex suggesting that eIF4B phosphorylation is key for the control of translation via HuD. To address this hypothesis, we are currently performing in vitro translation assays using HeLa cell extracts which are depleted of eIF4B. The status of these experiments will be discussed.