Lebedev M, Chan FY, Lochner A, Bellessem J, Osório DS, Rackles E, Mikeladze-Dvali T, Carvalho AX, Zanin E (2023)
Publication Type: Journal article
Publication year: 2023
Book Volume: 42
Article Number: 113076
Journal Issue: 9
DOI: 10.1016/j.celrep.2023.113076
During cytokinesis, a contractile ring consisting of unbranched filamentous actin (F-actin) and myosin II constricts at the cell equator. Unbranched F-actin is generated by formin, and without formin no cleavage furrow forms. In Caenorhabditis elegans, depletion of septin restores furrow ingression in formin mutants. How the cleavage furrow ingresses without a detectable unbranched F-actin ring is unknown. We report that, in this setting, anillin (ANI-1) forms a meshwork of circumferentially aligned linear structures decorated by non-muscle myosin II (NMY-2). Analysis of ANI-1 deletion mutants reveals that its disordered N-terminal half is required for linear structure formation and sufficient for furrow ingression. NMY-2 promotes the circumferential alignment of the linear ANI-1 structures and interacts with various lipids, suggesting that NMY-2 links the ANI-1 network with the plasma membrane. Collectively, our data reveal a compensatory mechanism, mediated by ANI-1 linear structures and membrane-bound NMY-2, that promotes furrowing when unbranched F-actin polymerization is compromised.
APA:
Lebedev, M., Chan, F.-Y., Lochner, A., Bellessem, J., Osório, D.S., Rackles, E.,... Zanin, E. (2023). Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion. Cell Reports, 42(9). https://dx.doi.org/10.1016/j.celrep.2023.113076
MLA:
Lebedev, Mikhail, et al. "Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion." Cell Reports 42.9 (2023).
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