دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion.
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
الوصف
تدمد:2211-1247
DOI:10.1016/j.celrep.2023.113076