The AAA-ATPase VCP sustains sarcoplasmic proteostasis, in part, by controlling autophagosome-lysosome fusion and the integrity of a dynamic tubular lysosomal network.

Experiments with mammalian cells and Xenopus egg extracts elucidate how three proteins cooperate to shape the reticular endoplasmic reticulum network.

Immunoisolation combined with quantitative proteomics identifies 79 proteins enriched in the tubular endoplasmic reticulum and provides useful tool for analyzing this organelle's functions.

Proteins of the reticulon and REEP families, homologous to the products of human Hereditary Spastic Paraplegia disease genes, contribute to shaping and continuity of the axonal endoplasmic reticulum network in Drosophila.

Cells in the tracheal systems of fruit fly larvae are organised into compartments with precisely located boundaries, which pattern the formation of branched tubular networks.

Lamellar and tubular cristae in mitochondria form by two different molecular pathways that form both involve F₁F_O-ATP synthase dimers and the MICOS complex, but formation of lamellar cristae also relies on Mgm1/Opa1.

In contrast to current knowledge that predicts that apicomplexan actin is unconventional, use of Chromobodies demonstrate that Toxoplasma F-actin forms a long, stable, highly dynamic tubular network that is required for material transfer and parasite maturation.

The endoplasmic reticulum (ER) uses ER tubules and specific ER autophagy machinery to prevent toxic, dominant-interfering, disease-causing, mutant proteins from entering the secretory pathway.

Kidney organoids are a high-fidelity system for investigating basement membrane regulation in development and disease.

Partially overlapping functions of a limited subset of actin binding proteins allow the parasite Toxoplasma gondii to achieve actin regulation required for complex cellular processes.