Analysis of aging yeast cells using the in-vivo roGFP2-based probe reveals redox-dependent heterogeneity, reflected in a bi-modal distribution of the oxidation status, differential growth and replication, as well as distinct proteomic and transcriptomic profiles.
The use of genetically encoded redox sensors in phagocytized bacteria reveals that, among the toxic cocktail of oxidants released into the neutrophil's phagolysosome, HOCl is the main component responsible for the oxidative modification of bacterial protein thiols.
In C. elegans, presenilin functions, independent of its gamma-secretase proteolytic activity, to regulate mitochondrial metabolism by controlling ER-mitochondrial calcium transfer and, even in the absence of Abeta signaling, loss of this activity leads to neurodegeneration.
Reactive oxygen species, previously considered damaging agents linked to pathology, are required for normal neuronal plasticity, including adjustment of synaptic terminal size, maintenance of synaptic physiology and adaptive behavioural responses.
The organization of layered/laminated axon projections in specific regions of the fruitfly central brain is regulated by short-range repulsive guidance and is critical for local inhibitory circuit formation and function.
Phosphoproteomics identifies β-arrestin 2 phosphorylation at Thr383 by MEK as a key step of GPCR-induced Erk½ activation, thus providing new insight into the molecular mechanism underlying β-arrestin-dependent GPCR-operated signaling.
In mouse models of Huntington's disease, the subthalamic nucleus, which suppresses movements, also exhibits impaired glutamate homeostasis, NMDA receptor-dependent mitochondrial oxidant stress, firing disruption, and 30% neuronal loss.
The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.
Adapting a cytosolic enzyme that breaks down glutathione to function in the lumen of the endoplasmic reticulum challenges the long-held view that reduced glutathione fuels disulfide rearrangements during protein folding.