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Reverte-López, M.* ; Kanwa, N.* ; Qutbuddin, Y.* ; Belousova, V.* ; Jasnin, M. ; Schwille, P.*

Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division.

Nat. Commun. 15:10415 (2024)
Verlagsversion DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
A key challenge for bottom-up synthetic biology is engineering a minimal module for self-division of synthetic cells. Actin-based cytokinetic rings are considered a promising structure to produce the forces required for the controlled excision of cell-like compartments such as giant unilamellar vesicles (GUVs). Despite prior demonstrations of actin ring targeting to GUV membranes and myosin-induced constriction, large-scale vesicle deformation has been precluded due to the lacking spatial control of these contractile structures. Here we show the combined reconstitution of actomyosin rings and the bacterial MinDE protein system within GUVs. Incorporating this spatial positioning tool, able to induce active transport of membrane-attached diffusible molecules, yields self-organized equatorial assembly of actomyosin rings in vesicles. Remarkably, the synergistic effect of Min oscillations and the contractility of actomyosin bundles induces mid-vesicle deformations and vesicle blebbing. Our system showcases how functional machineries from various organisms may be combined in vitro, leading to the emergence of functionalities towards a synthetic division system.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Membrane Curvature; Giant Vesicles; Mind; Dynamics; Reconstitution; Phase
Sprache englisch
Veröffentlichungsjahr 2024
HGF-Berichtsjahr 2024
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Zeitschrift Nature Communications
Quellenangaben Band: 15, Heft: 1, Seiten: , Artikelnummer: 10415 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed
Institut(e) Helmholtz Pioneer Campus (HPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Pioneer Campus
PSP-Element(e) G-510008-001
Förderungen Projekt DEAL
Scopus ID 85211158937
PubMed ID 39614082
Erfassungsdatum 2024-12-04