ArticleProceedings of the National Academy of Sciences of the United States of America2022
The endoplasmic reticulum adopts two distinct tubule forms.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed.
- Phenoxazines with a PhototransferableJournal of the American Chemical Society · 2026Article
- Interferometric ultra-high resolution 3D imaging through brain sections.Nature communications · 2026Article
- Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress.bioRxiv : the preprint server for biology · 2026Article
- Designing chemigenetic DNA nanotrap for norepinephrine dynamic imaging in organelles.Nature chemical biology · 2026Article
- Nanoscale Mapping of the Subcellular Glycosylation Landscape.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Controlling Intramolecular Rotation with Five-Membered Heterocycles Facilitates the Design of Highly Cell-Permeable Xanthene-Based Fluorogenic Probes.Journal of the American Chemical Society · 2025Article
- There and back again: a cell biologist's journey from organelles to molecules.Biological chemistry · 2025Review
- Direct microsecond wide-field single-molecule tracking and super-resolution mapping via CCD vertical shift.Nature communications · 2025Article
- nERdy: network analysis of endoplasmic reticulum dynamics.Communications biology · 2025Article
- Fast and robust drift correction for single-molecule localization microscopy.Nature communications · 2025Article
- Self-cleavage of the GAIN domain of adhesion G protein-coupled receptors requires multiple domain-extrinsic factors.Nature communications · 2025Article
- Article
- The endoplasmic reticulum as an active liquid network.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Immunocytochemistry of Primary Cultured Cerebral Cortical Neurons.Methods in molecular biology (Clifton, N.J.) · 2024Article
- iU-ExM: nanoscopy of organelles and tissues with iterative ultrastructure expansion microscopy.Nature communications · 2023Article
- The nanoscale organization of reticulon 4 shapes local endoplasmic reticulum structure in situ.The Journal of cell biology · 2023Article
- Assessing crosstalk in simultaneous multicolor single-molecule localization microscopy.Cell reports methods · 2023Article
- Endoplasmic reticulum network heterogeneity guides diffusive transport and kinetics.Biophysical journal · 2023Article
- Structural Diversity within the Endoplasmic Reticulum-From the Microscale to the Nanoscale.Cold Spring Harbor perspectives in biology · 2023Review
- The nanoscale organization of reticulon 4 shapes local endoplasmic reticulum structurebioRxiv : the preprint server for biology · 2023Article
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Abstract
The endoplasmic reticulum (ER) is a versatile organelle with diverse functions. Through superresolution microscopy, we show that the peripheral ER in the mammalian cell adopts two distinct forms of tubules. Whereas an ultrathin form, R1, is consistently covered by ER-membrane curvature-promoting proteins, for example, Rtn4 in the native cell, in the second form, R2, Rtn4 and analogs are arranged into two parallel lines at a conserved separation of ∼105 nm over long ranges. The two tubule forms together account for ∼90% of the total tubule length in the cell, with either one being dominant in different cell types. The R1–R2 dichotomy and the final tubule geometry are both coregulated by Rtn4 (and analogs) and the ER sheet–maintaining protein Climp63, which, respectively, define the edge curvature and lumen height of the R2 tubules to generate a ribbon-like structure of well-defined width. Accordingly, the R2 tubule width correlates positively with the Climp63 intraluminal size. The R1 and R2 tubules undergo active remodeling at the second/subsecond timescales as they differently accommodate proteins, with the former effectively excluding ER-luminal proteins and ER-membrane proteins with large intraluminal domains. We thus uncover a dynamic structural dichotomy for ER tubules with intriguing functional implications.
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