دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: β-heavy-spectrin stabilizes the constricting contractile ring during cytokinesis.
المؤلفون: 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.
المصدر: The Journal of cell biology [J Cell Biol] 2023 Jan 02; Vol. 222 (1). Date of Electronic Publication: 2022 Oct 11.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Rockefeller University Press Country of Publication: United States NLM ID: 0375356 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1540-8140 (Electronic) Linking ISSN: 00219525 NLM ISO Abbreviation: J Cell Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: New York : Rockefeller University Press
مواضيع طبية MeSH: Actin Cytoskeleton* , Cytokinesis* , Spectrin*/metabolism, Actins ; Actomyosin ; Animals ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans Proteins/metabolism ; Formins ; Membrane Glycoproteins/metabolism ; Membrane Proteins/metabolism ; Microfilament Proteins/metabolism
مستخلص: 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.)
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المشرفين على المادة: 0 (Actins)
0 (Caenorhabditis elegans Proteins)
0 (Formins)
0 (Membrane Glycoproteins)
0 (Membrane Proteins)
0 (Microfilament Proteins)
0 (SMA-1 protein, C elegans)
0 (plastin)
12634-43-4 (Spectrin)
9013-26-7 (Actomyosin)
تواريخ الأحداث: Date Created: 20221011 Date Completed: 20221013 Latest Revision: 20230412
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9559602
DOI: 10.1083/jcb.202202024
PMID: 36219157
قاعدة البيانات: MEDLINE
الوصف
تدمد:1540-8140
DOI:10.1083/jcb.202202024