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

MakA, a pore-forming cytotoxin produced by Vibrio cholerae, forms oligomers and remodels membranes into high-curvature tubes, resulting in membrane integrity loss inside acidified organelle lumens or when cultured with cells in an acidic medium.

The autophagy protein ATG2A tethers membranes and transfers lipids between them, suggesting that autophagosome membranes grow upon the acquisition of lipids from the ER through the ATG2A bridge.

Based on two independent methods, mitochondria operate at temperatures up to 15°C hotter than ambient, adjusting their heat production so as to maintain temperature in face of physiological stresses.

Intracellular growth of the bacterial pathogen Legionella pneumophila in the amoeba Dictyostelium discoideum implicates a bacterial fatty acid transporter as well as dynamic interactions of the distinct membrane-bound replication compartment with host cell lipid droplets.

Identification of novel vesicular transporters will shed light on to expanding the chemical diversity of neurotransmitters or neuromodulators.

The mechanism is revealed that connects the protein degradation machinery to cellular membrane-bound compartments during proteostasis stress in mammalian cells.

An atypical neuronal pacemaker mechanism triggers feeding motor pattern in Aplysia..

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

Live-cell nanometer-resolution RNA labeling method enables transcriptome-wide mapping of endogenous RNAs in nuclear, cytosol, ER, and mitochondrial subcompartments.