Ishikawa et al. establish a comprehensive resource of strains and plasmids to suppress genes required for fission yeast viability. Strains and plasmids are individually stored, and they enable complicated phenotypical analyses, facilitating functional investigations of essential genes that are evolutionary conserved among eukaryotes.

While previous work suggested that Dachsous promotes growth via the Hippo pathway and Fat represses it, Matakatsu and Fehon show that these proteins function together to restrict growth by coordinately removing a “core complex” consisting of Dachs, Dlish, and Approximated from the junctional cortex.

Du et al. identify Sec23IP as an adaptor that recruits VPS13B to ER exit site–Golgi interfaces, and the interaction is required for the formation of tubular ERGIC and efficient ER export of procollagen. These findings reveal a role of VPS13B–Sec23IP interaction in Cohen syndrome pathogenesis.

Axonal regeneration is an energy-demanding process. Masin et al. show that in Pten and Socs3 co-deleted retinal ganglion cells, axonal regrowth requires and is fueled by a local axonal upregulation of glycolysis. Its targeting could provide new therapeutic avenues to induce axonal regrowth.

Silverman et al. leveraged advanced light and electron microscopy to perform quantitative morphometry of the intestinal tuft cell cytoskeleton. Three-dimensional reconstructions of segmented image data reveal a co-aligned actin–microtubule superstructure that may play a fundamental role in tuft cell function.

This study unveils migratory autolysosome disposal, a response to lysosomal damage where cells expel LAMP1-LC3 positive structures via autolysosome exocytosis, requiring autophagy machinery, SNARE proteins, and cell migration. This novel mechanism highlights the intricate relationship between cell migration, organelle quality control, and extracellular vesicle release.

Ugur et al. characterize the bridge-like lipid transfer protein VPS13B and report its localization between Golgi cisternae and its impact on Golgi complex reformation after its BFA-induced dispersion. They also provide evidence for its functional partnership with FAM177A1, a newly identified Golgi complex protein.