3D pattern formation of a protein–membrane suspension

Journal Article · Fri Sep 12 00:00:00 UTC 2025 · Proceedings of the National Academy of Sciences of the United States of America

DOI: https://doi.org/10.1073/pnas.2506401122 · OSTI ID:3251269

Chardac, Amélie  ^[1]; Norton, Michael M.  ^[1]; Touboul, Jonathan  ^[1]; Duclos, Guillaume  ^[1]

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1. Brandeis University, Waltham, MA (United States)

Many essential cellular processes, including cell division and the establishment of cell polarity during embryogenesis, are regulated by pattern-forming proteins. These proteins often need to bind to a substrate, such as the cell membrane, onto which they interact and form two-dimensional (2D) patterns. It is unclear how the membrane’s continuity and dimensionality impact pattern formation. Here, we address this gap using the MinDE system, a prototypical example of pattern-forming membrane proteins. We show that when the lipid substrate is fragmented into submicrometer-sized diffusive liposomes, adenosine triphosphate-driven protein–protein interactions generate three-dimensional (3D) spatially extended patterns, despite the complete loss of membrane continuity. Remarkably, these 3D patterns emerge at scales four orders of magnitude larger than the individual liposomes. By systematically varying protein concentration, liposome size, and density, we observed and characterized a variety of 3D dynamical patterns not seen on continuous 2D membranes, including traveling waves, dynamical spirals, and a coexistence phase. Simulations and linear stability analysis of a coarse-grained model revealed that the physical properties of the dispersed membrane effectively rescale both the protein–membrane binding rates and diffusion, two key parameters governing pattern formation and wavelength selection. These findings highlight the robustness of Min’s pattern-forming ability, suggesting that protein–membrane suspensions could serve as an adaptable template for studying out-of-equilibrium self-organization in 3D, beyond in vivo contexts.

• Research Organization: University of Nebraska, Lincoln, NE (United States); University of Nebraska-Lincoln, NE (United States)
• Sponsoring Organization: National Science Foundation (NSF); USDOE Office of Science (SC), Basic Energy Sciences (BES)
• Grant/Contract Number: SC0022280
• OSTI ID: 3251269
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 37 Vol. 122; ISSN 1091-6490; ISSN 0027-8424
• Publisher: National Academy of SciencesCopyright Statement
• Country of Publication: United States
• Language: English