دورية أكاديمية
أعرض في EDS

Rapid assembly of a polar network architecture drives efficient actomyosin contractility.

التفاصيل البيبلوغرافية
العنوان: Rapid assembly of a polar network architecture drives efficient actomyosin contractility.
المؤلفون: Costache V; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France., Prigent Garcia S; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France., Plancke CN; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France., Li J; Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN, USA., Begnaud S; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France., Suman SK; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France., Reymann AC; IGBMC, CNRS UMR7104, INSERM U1258, and Université de Strasbourg, Illkirch, France., Kim T; Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN, USA. Electronic address: kimty@purdue.edu., Robin FB; Sorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine IBPS, Laboratoire de Biologie du Développement, Paris, France. Electronic address: francois.robin@sorbonne-universite.fr.
المصدر: Cell reports [Cell Rep] 2022 May 31; Vol. 39 (9), pp. 110868.
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 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* , Actomyosin*, Actin Cytoskeleton ; Formins ; Muscle Contraction
مستخلص: Actin network architecture and dynamics play a central role in cell contractility and tissue morphogenesis. RhoA-driven pulsed contractions are a generic mode of actomyosin contractility, but the mechanisms underlying how their specific architecture emerges and how this architecture supports the contractile function of the network remain unclear. Here we show that, during pulsed contractions, the actin network is assembled by two subpopulations of formins: a functionally inactive population (recruited) and formins actively participating in actin filament elongation (elongating). We then show that elongating formins assemble a polar actin network, with barbed ends pointing out of the pulse. Numerical simulations demonstrate that this geometry favors rapid network contraction. Our results show that formins convert a local RhoA activity gradient into a polar network architecture, causing efficient network contractility, underlying the key function of kinetic controls in the assembly and mechanics of cortical network architectures.
Competing Interests: Declaration of interests The authors declare no competing interests.
(Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.)
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معلومات مُعتمدة: R01 GM126256 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: CP: cell biology; actomyosin; cell mechanics; cytoskeleton; formin; kinetics; live microscopy; mDia; numerical simulations; single-molecule microscopy
المشرفين على المادة: 0 (Actins)
0 (Formins)
9013-26-7 (Actomyosin)
تواريخ الأحداث: Date Created: 20220601 Date Completed: 20220603 Latest Revision: 20220906
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC9210446
DOI: 10.1016/j.celrep.2022.110868
PMID: 35649363
قاعدة البيانات: MEDLINE
الوصف
تدمد:2211-1247
DOI:10.1016/j.celrep.2022.110868