The ribosomal protein S6 kinases (S6K) are among the major substrates and crucial effectors of the target of rapamycin (TOR) kinase, which is an evolutionarily conserved regulator of cell growth and proliferation. Recent research indicates that yeast Ypk3 is an ortholog of mammalian S6Ks. Here, we find that plant S6Ks restore ribosomal protein S6 phosphorylation in a rapamycin-sensitive manner in yeast cells lacking Ypk3. However, phosphorylation of a hydrophobic motif, which is mediated through TOR signaling and essential for mammalian S6K activity, is not detected in plant S6Ks. Furthermore, deletion of the N-terminal region of rice S6Ks shows phosphorylation of the hydrophobic motif and reduced rapamycin sensitivity. Our findings suggest a mechanism of plant S6K activation distinct from that of mammalian S6Ks.

The S6 kinases (S6Ks) are known to be activated by the target of rapamycin through phosphorylation of their hydrophobic motif (HM). However, our previous research showed that the HM site of plant S6Ks is not phosphorylated and is not essential for their activity in yeast cells lacking Ypk3, an ortholog of mammalian S6K. Here, we demonstrate that the HM site of mammalian S6Ks is phosphorylated and is indispensable for their activity in yeast ypk3∆ cells. Furthermore, pseudo‐phosphorylation at the HM site of plant S6Ks results in regaining of activity that is lost due to mutation in the conserved phosphorylation sites, namely the T‐loop and Turn motif. These results indicate the activation mechanism of plant S6Ks is different from that of mammals.

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