ArticleThe Journal of biological chemistry2011
Membrane curvature sensing by amphipathic helices: a single liposome study using α-synuclein and annexin B12.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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74 citing papers in PubMed, 135 citations in OpenAlex.
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- Cholesterol modulates vesicle clustering mediated by alpha-synuclein in a nonlinear fashion.Biophysics reports · 2025Article
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- Saddle curvature association of nsP1 facilitates the replication complex assembly of Chikungunya virus in cells.Nature communications · 2025Article
- Charge distribution and helicity tune the binding of septin's amphipathic helix domain to membranes.Biophysical journal · 2025Article
- Viral Membrane-Targeting Amphipathic Helical Peptide-Based Fluorogenic Probes for the Analysis of Infectious Titers of Enveloped Viruses.Analytical chemistry · 2025Article
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- Investigating Complexin-Membrane Interactions Using NMR and Optical Methods.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Interactions of alpha-synuclein with membranes in Parkinson's disease: Mechanisms and therapeutic strategies.Neurobiology of disease · 2024Review
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- A live cell imaging-based assay for tracking particle uptake by clathrin-mediated endocytosis.Methods in enzymology · 2024Article
- Membrane Proteins and Membrane Curvature: Mutual Interactions and a Perspective on Disease Treatments.Biomolecules · 2023Review
- Article
- Physics-based generative model of curvature sensing peptides; distinguishing sensors from binders.Science advances · 2023Article
14 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Preferential binding of proteins on curved membranes (membrane curvature sensing) is increasingly emerging as a general mechanism whereby cells may effect protein localization and trafficking. Here we use a novel single liposome fluorescence microscopy assay to examine a common sensing motif, the amphipathic helix (AH), and provide quantitative measures describing and distinguishing membrane binding and sensing behavior. By studying two AH-containing proteins, α-synuclein and annexin B12, as well as a range of AH peptide mutants, we reveal that both the hydrophobic and hydrophilic faces of the helix greatly influence binding and sensing. Although increased hydrophobic and electrostatic interactions with the membrane both lead to greater densities of bound protein, the former yields membrane curvature-sensitive binding, whereas the latter is not curvature-dependent. However, the relative contributions of both components determine the sensing of AHs. In contrast, charge density in the lipid membrane seems important primarily in attracting AHs to the membrane but does not significantly influence sensing. These observations were made possible by the ability of our assay to distinguish within our samples liposomes with and without bound protein as well as the density of bound protein. Our findings suggest that the description of membrane curvature-sensing requires consideration of several factors such as short and long range electrostatic interactions, hydrogen bonding, and the volume and structure of inserted hydrophobic residues.
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