Regulation of protein synthesis is critical for maintaining cellular homeostasis. In mammalian systems， translational regulatory networks have been elucidated in considerable detail. In plants， however， regulation occurs through different mechanisms that remain largely elusive. In this study， we present evidence that the Arabidopsis thaliana energy sensing kinase SnRK1， a homologue of mammalian AMP-activated kinase and yeast sucrose non-fermenting 1 (SNF1)， inhibits translation by phosphorylating the cap binding proteins eIF4E and eIFiso4E. We establish that eIF4E and eIFiso4E contain two deeply conserved SnRK1 consensus target sites and that both interact with SnRK1 in vivo. We then demonstrate that SnRK1 phosphorylation inhibits the ability of Arabidopsis eIF4E and eIFiso4E to complement a yeast strain lacking endogenous eIF4E， and that inhibition correlates with repression of polysome formation. Finally， we show that SnRK1 over-expression in Nicotiana benthamiana plants reduces polysome formation， and that this effect can be counteracted by transient expression of eIF4E or mutant eIF4E containing non-phosphorylatable SnRK1 target residues， but not by a phosphomimic eIF4E. Together， these studies elucidate a novel and direct pathway for translational control in plant cells. In light of previous findings that SnRK1 conditions an innate antiviral defense and is inhibited by geminivirus pathogenicity factors， we speculate that phosphorylation of cap binding proteins may be a component of the resistance mechanism.