Bucciarelli et al. report that mutations in terno lead to a third meiotic division in Drosophila males. Terno interacts with cyclins A and B and the APC/C complex, and its loss increases the cyclin levels. This is likely to increase Cdk1-CycA and Cdk1-CycB activities, resulting in an extra meiotic division.

Ruault et al. reveal how budding yeast telomeres reorganize from peripheral foci to a central hypercluster in long-lived quiescent cells. They show that the sequential inactivation of nuclear envelope anchoring pathways after the diauxic shift drives this reorganization, linking metabolism and genome organization.

A scavenger receptor (CD44) and a receptor tyrosine kinase (EPHA2) join forces to mediate internalization of therapeutic ASOs into endosomes, which are then captured on the nuclear surface. Nuclear-captured endosomes become leaky, allowing ASO escape. This novel endocytic route provides insight into how ASO-mediated therapies may be optimized.

Nsamba and Villeneuve use high-resolution immunofluorescence microscopy and live imaging to investigate C. elegans oocyte meiosis, providing evidence for a model in which β-tubulin isotype composition helps to maintain a balance between microtubule-crosslinking and microtubule severing required for normal assembly and function of acentrosomal spindles.

Here, Sun et al. demonstrate that loss of the transcription factor STAT5A reduces α-actinin-1 expression, leading to collapse of the actin cytoskeleton. This disruption of cellular architecture alters organelle distribution, promoting mitochondrial ROS production, DNA damage, and cGAS activation, triggering innate immune responses, thus uncovering a key link between cytoskeletal integrity and innate immune regulation.

BDCPs represent a family of large membrane-associated transmembrane cargo adaptors. In the current study, Dahl et al. determined the cryo-EM structure of the full-length BEACH domain protein NBEAL2 and identified the N-terminal α-solenoid/concanavalin A–like domain assembly of the typical BDCPs NBEAL1, NBEAL2, LYST, ALFY, LRBA, and NBEA as a modular membrane recruitment domain.

Super-resolution imaging reveals that CAR-T cells assemble immunological synapses with distinct actin architectures, including reduced central clearance and enhanced protrusions, highlighting fundamental cytoskeletal differences from TCR-driven synapses that may shape CAR-T signaling dynamics, synapse stability, and effector function.