β-heavy-spectrin stabilizes the constricting contractile ring during cytokinesis.

Autor:	Silva AM; i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.; IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal., Chan FY; i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.; IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal., Norman MJ; Department of Physics, North Carolina State University, Raleigh, NC.; Quantitative and Computational Developmental Biology Cluster, North Carolina State University, Raleigh, NC., Sobral AF; i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.; IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal., Zanin E; Department Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany., Gassmann R; i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.; IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal., Belmonte JM; Department of Physics, North Carolina State University, Raleigh, NC.; Quantitative and Computational Developmental Biology Cluster, North Carolina State University, Raleigh, NC., Carvalho AX; i3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.; IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2023 Jan 02; Vol. 222 (1). Date of Electronic Publication: 2022 Oct 11.
DOI:	10.1083/jcb.202202024
Abstrakt:	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. (© 2022 Silva et al.)
Databáze:	MEDLINE
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