Activation of the integrated stress response by stalled translation elongation complexes attenuates neurodegeneration, and demonstrates a protective link between a decrease in the rate of translation initiation and defects in translation elongation.

The kinase that controls maternal mRNA translation is regulated by phosphorylation of its activating subunit to restrict kinase activity to the developmental window between meiosis completion and early embryogenesis.

Activation of the stress response pathway in young cells extends replicative lifespan, not by reducing global protein synthesis per se, but by Gcn4-mediated autophagy induction.

Tyramine-dependent signaling triggers decondensation of neuronal RNP components and rapid translation activation of target mRNAs.

Binding of the translation initiation factor eIF3 to the messenger RNAs encoding the T cell receptor subunits alpha and beta is required to drive a short burst in their translation and promote a strong T cell response.

Post-transcriptional regulation of Aurora Kinase A (AURKA) through alternative polyadenylation of its mRNA determines miRNA influence and is a feature of cell cycle-specific AURKA expression whose impairment leads to acquisition of cancer phenotypes.

By attenuating the translation of key mRNA targets, ZFP36 RNA binding proteins restrain the expansion and effector activity of T cells.

Experimental measurement of the trajectory of gating charge surrogates during voltage activation and deactivation in a voltage sensor.

The Drosophila PNG kinase controls mRNA translation at the oocyte-to-embryo transition, and its GNU activating subunit is shown here to bind translational repressors and be a component of RNP granules.