FtsZ Reorganization Facilitates Deformation of Giant Vesicles in Microfluidic Traps

• Published in: Angewandte Chemie International Edition Vol. 59; no. 48; pp. 21372 - 21376
• Main Authors: Ganzinger, Kristina A., Merino‐Salomón, Adrián, García‐Soriano, Daniela A., Butterfield, A. Nelson, Litschel, Thomas, Siedler, Frank, Schwille, Petra
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 23.11.2020; John Wiley and Sons Inc
• Edition: International ed. in English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; cell division; Communication; Communications; Compartments; Cytoskeletal Proteins - chemistry; Cytoskeletal Proteins - metabolism; Deformation; Filaments; Lab-On-A-Chip Devices; Membranes; Microfluidics; Proteins; protocells; Unilamellar Liposomes - chemistry; Unilamellar Liposomes - metabolism; Vesicles; membranes; cell division; protocells; microfluidics; vesicles
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.202001928

The geometry of reaction compartments can affect the local outcome of interface‐restricted reactions. Giant unilamellar vesicles (GUVs) are commonly used to generate cell‐sized, membrane‐bound reaction compartments, which are, however, always spherical. Herein, we report the development of a microfluidic chip to trap and reversibly deform GUVs into cigar‐like shapes. When trapping and elongating GUVs that contain the primary protein of the bacterial Z ring, FtsZ, we find that membrane‐bound FtsZ filaments align preferentially with the short GUV axis. When GUVs are released from this confinement and membrane tension is relaxed, FtsZ reorganizes reversibly from filaments into dynamic rings that stabilize membrane protrusions; a process that allows reversible GUV deformation. We conclude that microfluidic traps are useful for manipulating both geometry and tension of GUVs, and for investigating how both affect the outcome of spatially‐sensitive reactions inside them, such as that of protein self‐organization. Microfluidic vesicle traps were developed to trap and reversibly deform giant unilamellar vesicles (GUVs) and in doing so manipulate membrane geometry and tension. We use these traps to show that filaments of the bacterial cytoskeletal protein FtsZ orientate themselves along the short axis of elongated GUVs and that membrane tension drives reversible FtsZ reorganization from filaments into rings, which facilitates membrane shape changes.