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Anillin 形成线性结构，并在 septin 和 formin 耗竭后促进凹痕内陷。

Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion.

机构信息

Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Biologie, 91058 Erlangen, Germany; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany.

i3S - Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, 4200-135 Porto, Portugal; IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, 4200-135 Porto, Portugal.

出版信息

Cell Rep. 2023 Sep 26;42(9):113076. doi: 10.1016/j.celrep.2023.113076. Epub 2023 Sep 3.

DOI:10.1016/j.celrep.2023.113076
PMID:37665665
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10548094/
Abstract

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.

摘要

在胞质分裂过程中，由无分支丝状肌动蛋白 (F-actin) 和肌球蛋白 II 组成的收缩环在细胞赤道处收缩。无分支 F-actin 由formin 产生，没有 formin 就不会形成分裂沟。在秀丽隐杆线虫中， septin 的耗竭会恢复formin 突变体中的沟裂内陷。在没有可检测到的无分支 F-actin 环的情况下，分裂沟如何内陷是未知的。我们报告说，在这种情况下，膜联蛋白 (ANI-1) 形成了一个由沿圆周排列的线性结构组成的网格，这些结构由非肌肉肌球蛋白 II (NMY-2) 修饰。对 ANI-1 缺失突变体的分析表明，其无规则的 N 端半部分是线性结构形成所必需的，足以引起沟裂内陷。NMY-2 促进了线性 ANI-1 结构的圆周排列，并与各种脂质相互作用，表明 NMY-2 将 ANI-1 网络与质膜联系起来。总的来说，我们的数据揭示了一种补偿机制，由 ANI-1 线性结构和膜结合的 NMY-2 介导，当无分支 F-actin 聚合受到损害时，该机制促进了沟裂的形成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/482351c9c8e7/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/2af1d5841aea/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/006f39776f01/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/a585f3f2a20f/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/cec6feaebc5f/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/2912ee11b2ca/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/02aacad273fc/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/82450caa8fc4/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/482351c9c8e7/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/2af1d5841aea/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/006f39776f01/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/a585f3f2a20f/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/cec6feaebc5f/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/2912ee11b2ca/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/02aacad273fc/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/82450caa8fc4/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/df8a/10548094/482351c9c8e7/gr7.jpg

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iScience. 2023 May 19;26(6):106903. doi: 10.1016/j.isci.2023.106903. eCollection 2023 Jun 16.
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Cell Rep. 2022 Aug 30;40(9):111274. doi: 10.1016/j.celrep.2022.111274.
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Physical mechanisms of ESCRT-III-driven cell division.
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Mol Biol Cell. 2024 Jul 1;35(7):ar94. doi: 10.1091/mbc.E24-02-0096-T. Epub 2024 May 2.
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