Schneider and de Ruijter-Villani et al. demonstrate that two spindles assemble around the parental genomes in bovine zygotes even though, like human zygotes, they inherit centrioles from the sperm. The two independent microtubule arrays form by self-organization with only loosely connected centrosomes.

Nanba et al. demonstrate that the age-dependent decline of EGFR signaling impairs epidermal stem cell motility and reepithelialization through COL17A1 proteolysis. The resulting alteration of epidermal stem cell dynamics is involved in the decline of skin regenerative capacity with aging.

Kelly et al. identify the hypervariable region of atlastins as a partially structured segment that in human atlastin-1 contributes to membrane tethering efficiency and is a site for distinct phosphorylation events, suggesting a mode of regulation by post-translational modification of the enzyme in cells.

Bozkurt et al. find that besides activating apoptosis, TRAIL signaling induces entosis in colon cancer cells through TRAIL receptors and structural presence but not catalytic activity of caspase-8. Moreover, they provide evidence for an association of TRAIL signaling, cell-in-cell structures, and clinical outcome in CRC.

Ras GTPases are key membrane-associated elements of the EGFR-MAPK signaling pathway. Surve et al. demonstrate that endogenous KRAS and NRAS are predominantly localized to the plasma membrane and its tubular shaped protrusions and show that a small pool of surface EGFRs sustain signaling along the RAS-MAPK pathway, whereas internalized EGFRs do not significantly contribute to MAPK activity.

Kif18a mutant mice produce micronuclei following segregation of unaligned chromosomes but do not spontaneously form tumors. KIF18A KO cells form stable micronuclear envelopes around lagging chromosomes located near the spindle pole and outside the midzone. These data suggest stable micronuclei may not actively promote tumorigenesis.

Chen et al. provide a novel insight on how poly(PR) dipeptides from C9orf72 gene exert cytotoxicity. The alternate distribution of Arg facilitates multivalent protein–protein interactions with proteins harboring acidic motifs and disturbs their functions through entrapment in the phase-separated droplets.