ArticleLife science alliance2018
The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs.
Article in Life science alliance, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The trial behind it
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Who cites it
10 citing papers in PubMed.
- Built different: ER cisternae formed by the Arabidopsis Lunapark proteins differ in ultrastructure and affect ER-Golgi transport.The New phytologist · 2026Article
- Zika NS2B Protein: In Vitro Formation of Large Multimeric Networks.International journal of molecular sciences · 2026Article
- Yeast lunapark regulates the formation ofiScience · 2023Article
- A Plasmodium homolog of ER tubule-forming proteins is required for parasite virulence.Molecular microbiology · 2020Article
- Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast.Cells · 2020Review
- Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum.Communications biology · 2020Article
- Membrane and organelle dynamics during cell division.Nature reviews. Molecular cell biology · 2020Review
- Reciprocal regulation between lunapark and atlastin facilitates ER three-way junction formation.Protein & cell · 2019Article
- Article
- Mutations in LNPK, Encoding the Endoplasmic Reticulum Junction Stabilizer Lunapark, Cause a Recessive Neurodevelopmental Syndrome.American journal of human genetics · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Lunapark (Lnp) is a conserved membrane protein that localizes to and stabilizes three-way junctions of the tubular ER network. In higher eukaryotes, phosphorylation of Lnp may contribute to the conversion of the ER from tubules to sheets during mitosis. Here, we report on the reconstitution of purified Lnp with phospholipids. Surprisingly, Lnp induces the formation of stacked membrane discs. Each disc is a bicelle, with Lnp sitting in the bilayer facing both directions. The interaction between bicelles is mediated by the cytosolic domains of Lnp, resulting in a constant distance between the discs. A phosphomimetic Lnp mutant shows reduced bicelle stacking. Based on these results, we propose that Lnp tethers ER membranes in vivo in a cell cycle-dependent manner. Lnp appears to be the first membrane protein that induces the formation of stacked bicelles.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.