ArticleProceedings of the National Academy of Sciences of the United States of America2016
A C-terminal amphipathic helix is necessary for the in vivo tubule-shaping function of a plant reticulon.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- An ER-microtubule bridge: Reticulon 17 links microtubules with ER network organisation in plants.The Plant journal : for cell and molecular biology · 2026Article
- Built different: ER cisternae formed by the Arabidopsis Lunapark proteins differ in ultrastructure and affect ER-Golgi transport.The New phytologist · 2026Article
- Stromules: An Incident or Formalized Pathway for Molecules Transfer Between Organelles?International journal of molecular sciences · 2025Review
- RTN family and its response to abiotic stress in Oryza sativa.Scientific reports · 2025Article
- Endoplasmic reticulum membrane remodeling by targeting reticulon-4 induces pyroptosis to facilitate antitumor immune.Protein & cell · 2025Article
- Yop1 stability and membrane curvature generation propensity are controlled by its oligomerisation interface.The Biochemical journal · 2024Article
- The membrane curvature-inducing REEP1-4 proteins generate an ER-derived vesicular compartment.Nature communications · 2024Article
- Quantitation of ER Morphology and Dynamics.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Reticulons bind sphingolipids to activate the endoplasmic reticulum cell cycle checkpoint, the ER surveillance pathway.Cell reports · 2023Article
- Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants.Scientific reports · 2023Article
- RETICULON-LIKE PROTEIN B2 is a proviral factor co-opted for the biogenesis of viral replication organelles in plants.The Plant cell · 2023Article
- Structural Diversity within the Endoplasmic Reticulum-From the Microscale to the Nanoscale.Cold Spring Harbor perspectives in biology · 2023Review
- Fluorescence and phosphorescence lifetime imaging reveals a significant cell nuclear viscosity and refractive index changes upon DNA damage.Scientific reports · 2023Article
- Membrane contacts with the endoplasmic reticulum modulate plastid morphology and behaviour.Frontiers in plant science · 2023Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Characterization of interactions within the Igα/Igβ transmembrane domains of the human B-cell receptor provides insights into receptor assembly.The Journal of biological chemistry · 2022Article
- Exploring the eukaryotic Yip and REEP/Yop superfamily of membrane-shaping adapter proteins (MSAPs): A cacophony or harmony of structure and function?Frontiers in molecular biosciences · 2022Review
- Article
- Geometry and cellular function of organelle membrane interfaces.Plant physiology · 2021Review
- Curvature sensing amphipathic helix in the C-terminus of RTNLB13 is conserved in all endoplasmic reticulum shaping reticulons in Arabidopsis thaliana.Scientific reports · 2021Article
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Authors and funding
11 authors.
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Abstract
Reticulons (RTNs) are a class of endoplasmic reticulum (ER) membrane proteins that are capable of maintaining high membrane curvature, thus helping shape the ER membrane into tubules. The mechanism of action of RTNs is hypothesized to be a combination of wedging, resulting from the transmembrane topology of their conserved reticulon homology domain, and scaffolding, arising from the ability of RTNs to form low-mobility homo-oligomers within the membrane. We studied the plant RTN isoform RTN13, which has previously been shown to locate to ER tubules and the edges of ER cisternae and to induce constrictions in ER tubules when overexpressed, and identified a region in the C terminus containing a putative amphipathic helix (APH). Here we show that deletion of this region or disruption of the hydrophobic face of the predicted helix abolishes the ability of RTN13 to induce constrictions of ER tubules in vivo. These mutants, however, still retain their ability to interact and form low-mobility oligomers in the ER membrane. Hence, our evidence indicates that the conserved APH is a key structural feature for RTN13 function in vivo, and we propose that RTN, like other membrane morphogens, rely on APHs for their function.
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