Unknown

Dataset Information

0

Encapsulated actomyosin patterns drive cell-like membrane shape changes.


ABSTRACT: Cell shape changes from locomotion to cytokinesis are, to a large extent, driven by myosin-driven remodeling of cortical actin patterns. Passive crosslinkers such as α-actinin and fascin as well as actin nucleator Arp2/3 complex largely determine actin network architecture and, consequently, membrane shape changes. Here we reconstitute actomyosin networks inside cell-sized lipid bilayer vesicles and show that depending on vesicle size and concentrations of α-actinin and fascin actomyosin networks assemble into ring and aster-like patterns. Anchoring actin to the membrane does not change actin network architecture yet exerts forces and deforms the membrane when assembled in the form of a contractile ring. In the presence of α-actinin and fascin, an Arp2/3 complex-mediated actomyosin cortex is shown to assemble a ring-like pattern at the equatorial cortex followed by myosin-driven clustering and consequently blebbing. An active gel theory unifies a model for the observed membrane shape changes induced by the contractile cortex.

SUBMITTER: Bashirzadeh Y 

PROVIDER: S-EPMC9061794 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Encapsulated actomyosin patterns drive cell-like membrane shape changes.

Bashirzadeh Yashar Y   Moghimianavval Hossein H   Liu Allen P AP  

iScience 20220412 5


Cell shape changes from locomotion to cytokinesis are, to a large extent, driven by myosin-driven remodeling of cortical actin patterns. Passive crosslinkers such as α-actinin and fascin as well as actin nucleator Arp2/3 complex largely determine actin network architecture and, consequently, membrane shape changes. Here we reconstitute actomyosin networks inside cell-sized lipid bilayer vesicles and show that depending on vesicle size and concentrations of α-actinin and fascin actomyosin network  ...[more]

Similar Datasets

| S-EPMC3763371 | biostudies-literature
| S-EPMC6171965 | biostudies-literature
| S-EPMC5062568 | biostudies-literature
| S-EPMC5385936 | biostudies-literature
| S-EPMC2901438 | biostudies-literature
| S-EPMC5316839 | biostudies-literature
| S-EPMC4812753 | biostudies-literature
| S-EPMC3298882 | biostudies-literature
| S-EPMC5440693 | biostudies-literature
| S-EPMC1366569 | biostudies-literature