ArticleSoft matter2019
Structured and intrinsically disordered domains within Amphiphysin1 work together to sense and drive membrane curvature.
Article in Soft matter, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Subdomains of endophilin can drive membrane remodeling and facilitate controlled membrane scission.Biophysical journal · 2026Article
- The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026Article
- Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026Article
- Subdomains of Endophilin-NBAR Can Synergistically Drive Membrane Remodeling and Facilitate Controlled Membrane Scission.bioRxiv : the preprint server for biology · 2026Article
- Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity.Cellular and molecular life sciences : CMLS · 2025Article
- Epsin1 enforces a condensation-dependent checkpoint for ubiquitylated cargo during clathrin-mediated endocytosis.Nature communications · 2025Article
- Characterization of atypical BAR domain-containing proteins coded by Toxoplasma gondii.The Journal of biological chemistry · 2024Article
- Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Graphene Quantum Dots Inhibit Lipid Peroxidation in Biological Membranes.ACS applied bio materials · 2024Article
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis.Nature communications · 2023Article
- Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023Review
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Molecular Shape Solution for Mesoscopic Remodeling of Cellular Membranes.Annual review of biophysics · 2022Review
- Coding variants identified in patients with diabetes alter PICK1 BAR domain function in insulin granule biogenesis.The Journal of clinical investigation · 2022Article
- Observed steric crowding at modest coverage requires a particular membrane-binding scheme or a complementary mechanism.Biophysical journal · 2022Article
- Nanoarrays of Individual Liposomes and Bacterial Outer Membrane Vesicles by Liftoff Nanocontact Printing.Small (Weinheim an der Bergstrasse, Germany) · 2021Article
- Clathrin senses membrane curvature.Biophysical journal · 2021Article
- Comparative Study of Curvature Sensing Mediated by F-BAR and an Intrinsically Disordered Region of FBP17.iScience · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cellular membranes undergo remodeling during many cellular processes including endocytosis, cytoskeletal protrusion, and organelle biogenesis. During these events, specialized proteins sense and amplify fluctuations in membrane curvature to create stably curved architectures. Amphiphysin1 is a multi-domain protein containing an N-terminal crescent-shaped BAR (Bin/Amphiphysin/Rvs) domain and a C-terminal domain that is largely disordered. When studied in isolation, the BAR domain of Amphiphysin1 senses membrane curvature and generates membrane tubules. However, the disordered domain has been largely overlooked in these studies. Interestingly, our recent work has demonstrated that the disordered domain is capable of substantially amplifying the membrane remodeling ability of the BAR domain. However, the physical mechanisms responsible for these effects are presently unclear. Here we elucidated the functional role of the disordered domain by gradually truncating it, creating a family of mutant proteins, each of which contained the BAR domain and a fraction of the disordered domain. Using quantitative fluorescence and electron microscopy, our results indicate that the disordered domain contributes to membrane remodeling by making it more difficult for the protein to bind to and assemble on flat membrane surfaces. Specifically, we found that the disordered domain began to significantly impact membrane remodeling when its projected area exceeded that of the BAR domain. Once this threshold was crossed, steric interactions with the membrane surface and with neighboring disordered domains gave rise to increased curvature sensing and membrane vesiculation, respectively. These findings provide insight into the synergy between structured and disordered domains, each of which play important biophysical roles in membrane remodeling.
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