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Verfasst von:Ding, Wei Yung [VerfasserIn]   i
 Nédélec, François [VerfasserIn]   i
Titel:Plastin increases cortical connectivity to facilitate robust polarization and timely cytokinesis
Verf.angabe:Wei Yung Ding, Hui Ting Ong, Yusuke Hara, Jantana Wongsantichon, Yusuke Toyama, Robert C. Robinson, François Nédélec, and Ronen Zaidel-Bar
Umfang:16 S.
Fussnoten:Gesehen am 22.10.2018
Titel Quelle:Enthalten in: The journal of cell biology
Jahr Quelle:2017
Band/Heft Quelle:216(2017), 5, S. 1371-1386
ISSN Quelle:1540-8140
Abstract:Ding et al. characterize the function of the F-actin bundling protein plastin in the Caenorhabditis elegans zygote. They demonstrate that plastin is important for optimal connectivity in the cortical actomyosin network that drives large-scale contractile processes such as polarization and cytokinesis., The cell cortex is essential to maintain animal cell shape, and contractile forces generated within it by nonmuscle myosin II (NMY-2) drive cellular morphogenetic processes such as cytokinesis. The role of actin cross-linking proteins in cortical dynamics is still incompletely understood. Here, we show that the evolutionarily conserved actin bundling/cross-linking protein plastin is instrumental for the generation of potent cortical actomyosin contractility in the Caenorhabditis elegans zygote. PLST-1 was enriched in contractile structures and was required for effective coalescence of NMY-2 filaments into large contractile foci and for long-range coordinated contractility in the cortex. In the absence of PLST-1, polarization was compromised, cytokinesis was delayed or failed, and 50% of embryos died during development. Moreover, mathematical modeling showed that an optimal amount of bundling agents enhanced the ability of a network to contract. We propose that by increasing the connectivity of the F-actin meshwork, plastin enables the cortex to generate stronger and more coordinated forces to accomplish cellular morphogenesis.
DOI:doi:10.1083/jcb.201603070
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Verlag: http://dx.doi.org/10.1083/jcb.201603070
 Verlag: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5412556/
 DOI: https://doi.org/10.1083/jcb.201603070
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1582151458
Verknüpfungen:→ Zeitschrift

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