β-heavy-spectrin stabilizes the constricting contractile ring during cytokinesis.
Silva AM, Chan FY, Norman MJ, Sobral AF, Zanin E, Gassmann R, Belmonte JM, Carvalho AX (2023)
Publication Status: Published
Publication Type: Journal article
Publication year: 2023
Journal
Book Volume: 222
Journal Issue: 1
Abstract
Cytokinesis requires the constriction of an actomyosin-based contractile ring and involves multiple F-actin crosslinkers. We show that partial depletion of the C. elegans cytokinetic formin generates contractile rings with low F-actin levels that constrict but are structurally fragile, and we use this background to investigate the roles of the crosslinkers plastin/PLST-1 and β-heavy-spectrin/SMA-1 during ring constriction. We show that the removal of PLST-1 or SMA-1 has opposite effects on the structural integrity of fragile rings. PLST-1 loss reduces cortical tension that resists ring constriction and makes fragile rings less prone to ruptures and regressions, whereas SMA-1 loss exacerbates structural defects, leading to frequent ruptures and cytokinesis failure. Fragile rings without SMA-1 or containing a shorter SMA-1, repeatedly rupture at the same site, and SMA-1::GFP accumulates at repair sites in fragile rings and in rings cut by laser microsurgery. These results establish that β-heavy-spectrin stabilizes the constricting ring and reveals the importance of β-heavy-spectrin size for network connectivity at low F-actin density.
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APA:
Silva, A.M., Chan, F.-Y., Norman, M.J., Sobral, A.F., Zanin, E., Gassmann, R.,... Carvalho, A.X. (2023). β-heavy-spectrin stabilizes the constricting contractile ring during cytokinesis. The Journal of Cell Biology, 222(1). https://dx.doi.org/10.1083/jcb.202202024
MLA:
Silva, Ana Marta, et al. "β-heavy-spectrin stabilizes the constricting contractile ring during cytokinesis." The Journal of Cell Biology 222.1 (2023).
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