Figure 5. Disorder mediates stress-induced translational silencing.

Stress granules, which contain RNA and protein in a membraneless condensed particle, form and coalesce in response to cellular stress, sequestering proteins, including the dual-specificity kinase DYRK3 and mTORC1, the cellular factor that activates translation¹⁰⁸. Translational silencing is mediated by DYRK3 under stress conditions in two ways, through stabilization of stress granules by the interaction of the disordered N-terminal tail, thus prolonging the sequestration of mTORC1. When cellular stress is relieved, DYRK3 and mTORC1 are released from the stress granules. Active DYRK3 acts as a kinase to phosphorylate PRAS40, relieving its inhibition of mTORC1 and allowing the resumption of protein synthesis. Figure adapted from ¹⁰⁸ with permission.