A common genomic deletion in various human cancers disrupts mitochondrial protein homeostasis in a way that might be targeted by existing drugs.

Fluorescence fluctuation spectroscopy is implemented for detection of up to four molecular species, allowing users to quantify molecular interactions and stoichiometry of multicomponent complexes in live cells, in a wide range of biological processes, from membrane signaling to viral assembly.

The scaffolding protein Oskar organizes two types of germ granules by phase transition within the same cell but with distinct morphologies, composition and biological functions.

Disruption of TFEB and TFE3 results in diminished p53 signaling capacity and altered cell cycle regulation under genotoxic stress conditions.

Accumulation of mutations in some cancers is correlated with an aberration of DNA repair and access of a DNA deaminase to normal genomic DNA.

Mitochondrial RNAs attach to chromatin and regulate nuclear transcription in endothelial stress response.

Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.

Chemotherapeutics altering DNA topology evoke RNA polymerase I inhibition, rDNA damage and consequent formation of PNAs that segregate persistent rDNA lesions from the active nucleolus, with implications for rDNA maintenance and design of new cancer treatment strategies targeting rDNA repair.