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.
The V600E mutation in BRAF is a cancer hot spot because it opens the activation segment through destabilization of autoinhibitory interactions, but it does not significantly impair folding of the inactive or active kinase domain.
Phosphorylation of Aurora A does not trigger a population shift to the active state as previously thought, but instead switches the kinase on by tuning the structure and dynamics of a dynamically sampled subpopulation.
Development of a real-time SnRK2 kinase FRET reporter reveals rapid SnRK2 activation by ABA, but not by Methyl-Jasmonate or elevated CO2, while directly demonstrating basal SnRK2 activity in guard cells.