دورية أكاديمية
Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion.
العنوان: | Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion. |
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المؤلفون: | Lebedev M; Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Biologie, 91058 Erlangen, Germany; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany., Chan FY; 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., Lochner A; Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Biologie, 91058 Erlangen, Germany., Bellessem J; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany., Osório DS; 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., Rackles E; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany., Mikeladze-Dvali T; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany., Carvalho AX; 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., Zanin E; Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Biologie, 91058 Erlangen, Germany; Department Biologie, Ludwig-Maximilians University, Munich, 82152 Planegg-Martinsried, Germany. Electronic address: esther.zanin@fau.de. |
المصدر: | Cell reports [Cell Rep] 2023 Sep 26; Vol. 42 (9), pp. 113076. Date of Electronic Publication: 2023 Sep 03. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural |
اللغة: | English |
بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 101573691 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2211-1247 (Electronic) NLM ISO Abbreviation: Cell Rep Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: [Cambridge, MA] : Cell Press, c 2012- |
مواضيع طبية MeSH: | Actins*/metabolism , Caenorhabditis elegans Proteins*/genetics , Caenorhabditis elegans Proteins*/metabolism , Contractile Proteins*, Animals ; Septins/genetics ; Septins/metabolism ; Formins/metabolism ; Cytokinesis/physiology ; Cell Membrane/metabolism ; Caenorhabditis elegans/metabolism ; Myosin Type II/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism |
مستخلص: | 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. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.) |
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معلومات مُعتمدة: | P40 OD010440 United States OD NIH HHS |
فهرسة مساهمة: | Keywords: C. elegans; CP: Cell biology; actin; anillin; cell division; contractile ring; cytokinesis; formin; intrinsically disordered; liquid-liquid phase separation; myosin |
المشرفين على المادة: | 0 (anillin) 0 (Actins) EC 3.6.1.- (Septins) 0 (Formins) EC 3.6.1.- (Myosin Type II) 0 (ANI-1 protein, C elegans) 0 (Microfilament Proteins) 0 (Caenorhabditis elegans Proteins) 0 (Contractile Proteins) |
تواريخ الأحداث: | Date Created: 20230904 Date Completed: 20240214 Latest Revision: 20240214 |
رمز التحديث: | 20240214 |
مُعرف محوري في PubMed: | PMC10548094 |
DOI: | 10.1016/j.celrep.2023.113076 |
PMID: | 37665665 |
قاعدة البيانات: | MEDLINE |
تدمد: | 2211-1247 |
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DOI: | 10.1016/j.celrep.2023.113076 |