ReviewBiochimica et biophysica acta. Biomembranes2023
Membrane reshaping by protein condensates.
Review in Biochimica et biophysica acta. Biomembranes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed.
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Patchy Membrane-Directed Multiphase Complex Coacervation.Journal of the American Chemical Society · 2026Article
- Lipid Composition Modulates Secondary Structure at the Biocondensate-Membrane Interface.bioRxiv : the preprint server for biology · 2026Article
- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- Physiological implications of phase separation in vesicle organization and trafficking.BMC biology · 2026Review
- Membrane Curvature and Cancer: Mechanisms, Implications, and Therapeutic Perspectives.Cancers · 2026Review
- From dynamic condensates to pathological assemblies: the phase behavior of tau andFrontiers in molecular neuroscience · 2026Review
- Ballistic Microscopy (BaM).bioRxiv : the preprint server for biology · 2025Article
- Lipid-Mediated Assembly of Biomolecular Condensates: Mechanisms, Regulation, and Therapeutic Implications.Biology · 2025Review
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.bioRxiv : the preprint server for biology · 2025Article
- The rheology and interfacial properties of biomolecular condensates.Biophysical reviews · 2025Review
- Adaptations of Bacterial Extracellular Vesicles in Response to Antibiotic Pressure.International journal of molecular sciences · 2025Review
- Review
- Lipid packing and cholesterol content regulate membrane wetting and remodeling by biomolecular condensates.Nature communications · 2025Article
- The mechanobiology of biomolecular condensates.Biophysics reviews · 2025Review
- Quantification of Biomolecular Condensate Volume Reveals Network Swelling and Dissolution Regimes during Phase Transition.Biomacromolecules · 2025Article
- Protein droplets spread to seal tight junctions.Nature · 2024Article
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- Probing the surface charge of condensates using microelectrophoresis.Nature communications · 2024Article
- Adhesion energy controls lipid binding-mediated endocytosis.Nature communications · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Proteins can organize into dynamic, functionally important assemblies on fluid membrane surfaces. Phase separation has emerged as an important mechanism for forming such protein assemblies on the membrane during cell signaling, endocytosis, and cytoskeleton regulation. Protein-protein phase separation thus adds novel fluid mosaics to the classical Singer and Nicolson model. Protein condensates formed in this process can modulate membrane morphologies. This is evident from recent reports of protein condensate-driven membrane reshaping in processes such as endocytosis, autophagosome formation, and protein storage vacuole morphogenesis in plants. Lateral phase separation (on the membrane surface) of peripheral curvature coupling proteins can modulate such membrane morphological transitions. Additionally, three-dimensional protein phase separation can result in droplets that through adhesion can affect membrane shape changes. How do these condensate-driven curvature generation mechanisms contrast with the classically recognized scaffolding and amphipathic helix insertion activities of specific membrane remodeling proteins? A salient feature of these condensate-driven membrane activities is that they depend upon both macroscopic features (such as interfacial energies of the condensate, membrane, and cytosol) as well as microscopic, molecular-level interactions (such as protein-lipid binding). This review highlights the current understanding of the mechanisms underlying curvature generation by protein condensates in various biological pathways.
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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.