Transmembrane coupling of liquid-like protein condensates

• Published in: Nature communications Vol. 14; no. 1; p. 8015
• Main Authors: Lee, Yohan, Park, Sujin, Yuan, Feng, Hayden, Carl C., Wang, Liping, Lafer, Eileen M., Choi, Siyoung Q., Stachowiak, Jeanne C.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 04-12-2023; Nature Publishing Group; Nature Portfolio
• Subjects: 14/19; 631/45/612/1237; 631/57/2269; 631/57/2270; 82/80; 82/83; Biological membranes; Cell membranes; Condensates; Coupling; Humanities and Social Sciences; Information transfer; Lipid membranes; Lipids; Liquid phases; Membrane proteins; Membranes; multidisciplinary; Phase separation; Proteins; Science; Science (multidisciplinary)
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-023-43332-w

Liquid-liquid phase separation of proteins occurs on both surfaces of cellular membranes during diverse physiological processes. In vitro reconstitution could provide insight into the mechanisms underlying these events. However, most existing reconstitution techniques provide access to only one membrane surface, making it difficult to probe transmembrane phenomena. To study protein phase separation simultaneously on both membrane surfaces, we developed an array of freestanding planar lipid membranes. Interestingly, we observed that liquid-like protein condensates on one side of the membrane colocalized with those on the other side, resulting in transmembrane coupling. Our results, based on lipid probe partitioning and mobility of lipids, suggest that protein condensates locally reorganize membrane lipids, a process which could be explained by multiple effects. These findings suggest a mechanism by which signals originating on one side of a biological membrane, triggered by protein phase separation, can be transferred to the opposite side.
Using a freestanding planar lipid membrane system, the authors show that liquid-like protein condensates on one side of a lipid membrane colocalize with those on the opposite side, suggesting a mechanism of information transfer across biological membranes.