Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress

. These 'rods' emerge from demixing of saturated lipids into solid-like domains - a previously unrecognised, large-scale endomembrane phase behaviour, fundamentally distinct from the transient liquid-ordered nanodomains of the plasma membrane. ER-tubulating reticulon-homology proteins are excluded from rods; their segregation drives progressive membrane flattening and ultimately multilayered wrapping. Surfactant-producing alveolar type-II lung cells, enriched in saturated lipids, form rods even at 37°C, demonstrating that native lipid metabolism can induce this transformation. This spatially organizing lipid-protein domain interplay may tune the ER tubule/sheet balance and provide a homeoviscous mechanism to preserve fluidity in the cholesterol-poor ER under thermal or metabolic stress.

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Publication Details

Journal
bioRxiv (Cold Spring Harbor Laboratory)
Published
2026-04-12
DOI
https://doi.org/10.64898/2026.04.09.717431
Primary Topic
Lipid Membrane Structure and Behavior
Type
article
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article

Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress

Ilya Levental, Heike Naumann, Robert-William Welke, Philipp Trnka et al.
bioRxiv (Cold Spring Harbor Laboratory)
Lipid Membrane Structure and Behavior
article

Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress

Ilya Levental, Heike Naumann, Robert-William Welke, Philipp Trnka, Melissa R. Mikolaj, Kedar Narayan, Oliver Rocks, Helge Ewers, Elmehdi Belbaraka, Paul M. Mueller, Nina Taudien, Bjoern Perder, Sophia Altinoluk, Finn Hartstein, Kandice R. Levental
article en

Abstract

. These 'rods' emerge from demixing of saturated lipids into solid-like domains - a previously unrecognised, large-scale endomembrane phase behaviour, fundamentally distinct from the transient liquid-ordered nanodomains of the plasma membrane. ER-tubulating reticulon-homology proteins are excluded from rods; their segregation drives progressive membrane flattening and ultimately multilayered wrapping. Surfactant-producing alveolar type-II lung cells, enriched in saturated lipids, form rods even at 37°C, demonstrating that native lipid metabolism can induce this transformation. This spatially organizing lipid-protein domain interplay may tune the ER tubule/sheet balance and provide a homeoviscous mechanism to preserve fluidity in the cholesterol-poor ER under thermal or metabolic stress.

bioRxiv (Cold Spring Harbor Laboratory)
Max Delbrück Center (DE), Frederick National Laboratory for Cancer Research (US), Berlin Institute of Health at Charité - Universitätsmedizin Berlin (DE), National Cancer Institute (US), Deutsches Diabetes-Zentrum e.V. (DE), German Center for Diabetes Research (DE), University Hospital Carl Gustav Carus (DE), Paul Langerhans Institute Dresden (DE), Heinrich Heine University Düsseldorf (DE), University of Virginia (US), Freie Universität Berlin (DE), Charité - Universitätsmedizin Berlin (DE)
Openalex Percentile: Top 23%
Lipid Membrane Structure and Behavior
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