Asuka Yamaguchi and Takeshi Sasamura et al. show that cell chirality arises from directional actin flows driven by class 1 myosins in Drosophila macrophages. Myo1D organizes polarized circular F-actin that Myo2 rotates clockwise, providing a molecular basis for cell chirality.

Tran et al. show that mammalian metaphase kinetochores undergo large-scale, complex, and elastic deformations under forces of different timescales, magnitudes, and directions. They demonstrate that condensin is required for kinetochore local structural organization and microtubule attachment under force.

Plasek-Hedge et al. show that Malat1, a lncRNA thought to be exclusively nuclear, highly abundant, and very stable, in fact localizes to the cytoplasm in early G1, where it is degraded at the onset of each cell cycle by a translation-mediated decay pathway.

Jana, Ngo et al. reveal that β1-integrin and the tetraspanins CD9, CD81, and CD151 link the surface receptor CD36 to cortical actin, thereby regulating its dynamic organization and signaling. With their many interactions, integrins and tetraspanins may link many receptors lacking actin-binding motifs to cortical actin.

Bartolutti et al. show that physiological function for the unfolded protein response differs dramatically from its canonical role in driving a transcriptional program. Instead, this Ire1-mediated response prevents aberrant endoplasmic reticulum (ER) structures and represses translation, which reduces protein translocation into the ER, allowing cells to enter the meiotic program.

A versatile optogenetic tool enables light-controlled manipulation of nuclear proteins and structures. Using NLS-LARIAT in Drosophila ovarian cells, the authors reveal how rapid inhibition and clustering of GFP-tagged nuclear factors regulate border cell migration, nuclear mechanics, and the cell-fate consequences of nuclear protein dosage.

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.