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  FtsZ Reorganization Facilitates Deformation of Giant Vesicles in Microfluidic Traps

Ganzinger, K. A., Merino-Salomon, A., Garcia-Soriano, D. A., Butterfield, N. A., Litschel, T., Siedler, F., et al. (2020). FtsZ Reorganization Facilitates Deformation of Giant Vesicles in Microfluidic Traps. Angewandte Chemie International Edition, 59(48), 21372-21376. doi:10.1002/anie.202001928.

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Genre: Journal Article
Subtitle : Communication

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© 2020 The Authors. Open access funding enabled and organized by Projekt DEAL.
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https://doi.org/10.1101/791459 (Preprint)
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A previous version of this manuscript has been deposited on a preprint server.

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 Creators:
Ganzinger, Kristina A.1, Author              
Merino-Salomon, Adrian1, Author              
Garcia-Soriano, Daniela A.1, Author              
Butterfield, Nelson A.1, Author              
Litschel, Thomas1, Author              
Siedler, Frank1, Author              
Schwille, Petra1, Author              
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: RING STRUCTURE; MEMBRANE; RECONSTITUTION; DIVISION; BIOLOGY; ZIPAChemistry; cell division; membranes; microfluidics; protocells; vesicles;
 Abstract: 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.

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Language(s): eng - English
 Dates: 2020-072020-11
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: We acknowledge the MPIB Biochemistry Core Facility for assistance in protein purification.
 Rev. Type: -
 Identifiers: ISI: 000569893600001
DOI: 10.1002/anie.202001928
 Degree: -

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Project name : Marie Skłodowska‐Curie grant agreement
Grant ID : 703132
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Angewandte Chemie International Edition
  Abbreviation : Angew. Chem., Int. Ed.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 59 (48) Sequence Number: - Start / End Page: 21372 - 21376 Identifier: ISSN: 1433-7851
CoNE: https://pure.mpg.de/cone/journals/resource/1433-7851