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| Item Type: | Preprint |
|---|---|
| Title: | Large-scale endoplasmic reticulum membrane solidification spatially organises proteins under thermal or metabolic stress |
| Creators: |
Müller, Paul M.  ORCID: https://orcid.org/0000-0001-9056-4114, Mikolaj, Melissa R., Belbaraka, Elmehdi, Hartstein, Finn, Altinoluk, Sophia, Perder, Björn, Trnka, Philipp, Welke, Robert-William, Naumann, Heike ORCID: https://orcid.org/0000-0003-3883-0432, Taudien, Nina, Kunz, Severine ORCID: https://orcid.org/0000-0002-0131-3506, Solimena, Michele ORCID: https://orcid.org/0000-0002-3653-8107, Levental, Ilya ORCID: https://orcid.org/0000-0002-1206-9545, Levental, Kandice R., Müller, Andreas ORCID: https://orcid.org/0000-0002-3560-5769, Ewers, Helge ORCID: https://orcid.org/0000-0003-3948-4332, Narayan, Kedar and Rocks, Oliver ORCID: https://orcid.org/0000-0001-6349-9193
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| Abstract: | Organelle homeostasis is a key determinant of cellular fitness, yet how cells remodel their membranes in response to environmental change remains unclear. Here, we identify a temperature- and lipid saturation-dependent transformation of endoplasmic reticulum membranes into giant, rigid, multilamellar tubes in cells and in vivo . 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. |
| Keywords: | Animals, Mice |
| Source: | bioRxiv |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Article Number: | 2026.04.09.717431 |
| Date: | 12 April 2026 |
| Official Publication: | https://doi.org/10.64898/2026.04.09.717431 |
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