Wozniak et al. define a novel connection between cleavage of the Rab7 adaptor protein, RILP, and exosome secretion. They demonstrate that inflammasome-mediated RILP cleavage influences sequence-specific miRNA loading into exosomes via interactions with unique cargo vesicles and association with RNA binding proteins.

Organelle inheritance in yeast is a balance between two opposing processes, retention and inheritance. Hulmes et al. propose a new model for peroxisome retention involving contact with the plasma membrane and identify the plasma membrane–peroxisome tether responsible.

Cell and tissue morphogenesis are fundamental during development. The authors previously characterized Slik kinase and its effector, moesin, as regulators of mitotic morphogenesis and epithelial integrity. Here, they identify dSTRIPAK as a new regulator of Slik localization to promote moesin activation and functions.

Naegleria diverged from the “yeast-to-human” lineage >1 billion years ago. Velle and Fritz-Laylin found that Naegleria, which lacks interphase microtubules, has a robust actin cytoskeletal repertoire and uses conserved, Arp2/3–derived actin networks to drive cell crawling and enhance phagocytosis. These findings support an evolutionarily ancient origin for these phenotypes.

Shard et al. show that the emergence of neural stem cells from the Drosophila optic lobe neuroepithelium is an EMT-like process involving tissue-wide coordination. Neuralized acts downstream of NSC fate acquisition to downregulate the Crumbs complex to facilitate epithelium remodeling.

During mitochondrial complex I (CI) assembly, independently formed assembly intermediates (AIs) merge with each other to form the mature complex. Murari et al. generate a toolbox of 21 antibodies to various mitochondrial proteins and use classical Drosophila genetics and immunoblotting of AIs to define AIF’s role in CI biogenesis.

GuA1-containing AMPA receptors play a key role in synaptic plasticity and cognition. Casas et al. demonstrate that the sensing of nutrients by CPT1C regulates the phosphatase activity of SAC1, and consequently PI(4)P levels, at the contact sites between the endoplasmic reticulum and the trans-Golgi network to control the trafficking of GluA1 receptors to the cell surface of neurons.