A mitochondria-based 'priming' of stemness happens by fine-tuned repression of the level or activity of the master regulator of mitochondrial fission, Drp1, which supports carcinogen-induced transformation in a keratinocyte model.

Ribosomal protein mutations, mutations that affect ribosomal RNA synthesis, or function of the mature ribosome, trigger a transcriptional response mediated by Xrp1 expression which reduces cellular translation via eIF2-alpha phosphorylation and renders cells liable to competition with wild-type neighbors.

A key cellular process is controlled by altering a balance, rather than through an off/on mechanism.

Genetic and cell biological analyses reveal a new role of Drp1 in postsynaptic endocytosis during brain development beyond mitochondrial division GTPase.

Tyrosine phosphorylation of the intracellular domain of LRP1 serves as a molecular switch to regulate cellular cholesterol homeostasis through nuclear hormone receptor-mediated regulation of the cellular cholesterol exporter ABCA1.

The transcription factor Xrp1 mediates a previously unrecognized branch of stress-response signaling, specifically as a downstream effector of eIF2alpha kinases.

Xrp1 contributes to cell competition as a heterodimer with the Drosophila C/EBP homolog Irbp18 and although rapidly evolving is itself conserved beyond Drosophila.

Bidirectional promoter activity, which is inherent to the promoters of selection cassettes used for genome editing, causes divergent transcription that can disrupt expression of genes neighboring cassette insertion sites, causing potent off-target effects.

An activator of branching nucleation by Arp2/3 complex directly synergizes with an activator of linear filament nucleation to initiate assembly of actin networks that drive endocytosis.

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.