Endoplasmic reticulum exit sites (ERES) are specialized ER subdomains that regulate the export of secreted cargo. This Roadmap explores how ERES integrate biochemical and mechanical signals to coordinate trafficking and proposes a multidisciplinary strategy to investigate their function, including in disease.

Endoplasmic reticulum exit sites (ERES) are specialized ER subdomains that regulate the export of secreted cargo. This Roadmap explores how ERES integrate biochemical and mechanical signals to coordinate trafficking and proposes a multidisciplinary strategy to investigate their function, including in disease.

Rawal et al. combine intracellular cartography and biophysical modelling to reveal how edge curvature governs endoplasmic reticulum (ER) morphology, showing that curvature-dependent ER reorganization ...

Trafficking from the endoplasmic reticulum to the Golgi apparatus comprises the first steps toward the correct localization of 30% of eukaryotic proteins. Coat protein complexes COPII and COPI are inv...

Nature Structural & Molecular Biology, Published online: 14 July 2025; doi:10.1038/s41594-025-01619-0BiP–glucose-regulated protein 94 chaperones are critical to the proper folding of secretory and transmembrane proteins. Brenner et al. provide biochemical and structural insight into a conserved mechanism of chaperone cooperation underlying this quality control process.

SLC35B1, initially thought to be a nucleotide sugar transporter, is an essential ATP/ADP exchanger that imports ATP into the endoplasmic reticulum through a unique stepwise translocation mechanism.

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The advent of clonal multicellularity is a critical evolutionary milestone, seen often in eukaryotes, rarely in bacteria, and only once in archaea. We show that uniaxial compression induces clonal mul...