Journal
BIOPHYSICAL JOURNAL
Volume 117, Issue 3, Pages 553-562Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2019.06.025
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Funding
- National Institute of General Medical Sciences of the United States NIH [R01-GM063796]
- Human Frontiers Science Program [RGP0005/2016]
- European Molecular Biology Organization Long-Term fellowship [ALTF 1527-2014]
- Marie Curie actions (H2020-MSCA-IF-2014, project membrane-ezrin-actin)
- Labex CelTisPhyBio [ANR-11-LABX0038]
- Ruth L. Kirschstein National Research Service Award Postdoctoral Fellowship from the National Institute of General Medical Sciences of the NIH [F32-GM125218]
- National Science Foundation [ACI-1548562]
- Cell and Tissue Imaging (The BioImaging Cell and Tissue Core Facility of the Institut Curie), Institut Curie [ANR10-INBS-04]
- Paris Sciences et Lettres [ANR-10-IDEX-0001-02]
- France and Chicago Collaborating in the Sciences grant
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Protein-mediated membrane remodeling is a ubiquitous and critical process for proper cellular function. Inverse Bin/Amphiphysin/Rvs (I-BAR) domains drive local membrane deformation as a precursor to large-scale membrane remodeling. We employ a multiscale approach to provide the molecular mechanism of unusual I-BAR domain-driven membrane remodeling at a low protein surface concentration with near-atomistic detail. We generate a bottom-up coarse-grained model that demonstrates similar membrane-bound I-BAR domain aggregation behavior as our recent Mesoscopic Membrane with Explicit Proteins model. Together, these models bridge several length scales and reveal an aggregation behavior of I-BAR domains. We find that at low surface coverage (i.e., low bound protein density), I-BAR domains form transient, tip-to-tip strings on periodic flat membrane sheets. Inside of lipid bilayer tubules, we find linear aggregates parallel to the axis of the tubule. Finally, we find that I-BAR domains form tip-to-tip aggregates around the edges of membrane domes. These results are supported by in vitro experiments showing low curvature bulges surrounded by I-BAR domains on giant unilamellar vesicles. Overall, our models reveal new I-BAR domain aggregation behavior in membrane tubules and on the surface of vesicles at low surface concentration that add insight into how I-BAR domain proteins may contribute to certain aspects of membrane remodeling in cells.
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