Optogenetic relaxation of actomyosin contractility uncovers mechanistic roles of cortical tension during cytokinesis.
Actin Cytoskeleton
/ metabolism
Actomyosin
/ metabolism
Animals
Cell Membrane
/ metabolism
Cell Movement
Cytokinesis
/ genetics
Cytoskeletal Proteins
/ metabolism
Dogs
Female
Intercellular Junctions
Madin Darby Canine Kidney Cells
Male
Mechanical Phenomena
Morphogenesis
Muscle Contraction
Myosin Type II
/ metabolism
Myosin-Light-Chain Phosphatase
/ metabolism
Optogenetics
Synthetic Biology
Xenopus
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
08 12 2021
08 12 2021
Historique:
received:
04
05
2021
accepted:
17
11
2021
entrez:
9
12
2021
pubmed:
10
12
2021
medline:
11
1
2022
Statut:
epublish
Résumé
Actomyosin contractility generated cooperatively by nonmuscle myosin II and actin filaments plays essential roles in a wide range of biological processes, such as cell motility, cytokinesis, and tissue morphogenesis. However, subcellular dynamics of actomyosin contractility underlying such processes remains elusive. Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane. Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos. The OptoMYPT system is further employed to understand the mechanics of actomyosin-based cortical tension and contractile ring tension during cytokinesis. We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate, revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow. Based on these results, the OptoMYPT system provides opportunities to understand cellular and tissue mechanics.
Identifiants
pubmed: 34880255
doi: 10.1038/s41467-021-27458-3
pii: 10.1038/s41467-021-27458-3
pmc: PMC8654997
doi:
Substances chimiques
Cytoskeletal Proteins
0
Actomyosin
9013-26-7
Myosin-Light-Chain Phosphatase
EC 3.1.3.53
PPP1R12A protein, human
EC 3.1.3.53
Myosin Type II
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7145Informations de copyright
© 2021. The Author(s).
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