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Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division

During cytokinesis, the chromosomal passenger complex (CPC) promotes midzone organization, specifies the cleavage plane, and regulates furrow contractility. The localizations of the CPC are coupled to its cytokinetic functions. At the metaphase-to-anaphase transition, the CPC dissociates from centro...

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Autores principales: Landino, Jennifer, Norris, Stephen R., Li, Muyi, Ballister, Edward R., Lampson, Michael A., Ohi, Ryoma
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706991/
https://www.ncbi.nlm.nih.gov/pubmed/28954866
http://dx.doi.org/10.1091/mbc.E17-06-0399
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author Landino, Jennifer
Norris, Stephen R.
Li, Muyi
Ballister, Edward R.
Lampson, Michael A.
Ohi, Ryoma
author_facet Landino, Jennifer
Norris, Stephen R.
Li, Muyi
Ballister, Edward R.
Lampson, Michael A.
Ohi, Ryoma
author_sort Landino, Jennifer
collection PubMed
description During cytokinesis, the chromosomal passenger complex (CPC) promotes midzone organization, specifies the cleavage plane, and regulates furrow contractility. The localizations of the CPC are coupled to its cytokinetic functions. At the metaphase-to-anaphase transition, the CPC dissociates from centromeres and localizes to midzone microtubules and the equatorial cortex. CPC relocalization to the cell middle is thought to depend on MKlp2-driven, plus end–directed transport. In support of this idea, MKlp2 depletion impairs cytokinesis; however, cytokinesis failure stems from furrow regression rather than failed initiation of furrowing. This suggests that an alternative mechanism(s) may concentrate the CPC at the division plane. We show here that direct actin binding, via the inner centromere protein (INCENP), enhances CPC enrichment at the equatorial cortex, thus acting in tandem with MKlp2. INCENP overexpression rescues furrowing in MKlp2-depleted cells in an INCENP-actin binding–dependent manner. Using live-cell imaging, we also find that MKlp2-dependent targeting of the CPC is biphasic. MKlp2 targets the CPC to the anti-parallel microtubule overlap of the midzone, after which the MKlp2-CPC complex moves in a nondirected manner. Collectively, our work suggests that both actin binding and MKlp2-dependent midzone targeting cooperate to precisely position the CPC during mitotic exit, and that these pathways converge to ensure successful cleavage furrow ingression.
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spelling pubmed-57069912018-02-16 Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division Landino, Jennifer Norris, Stephen R. Li, Muyi Ballister, Edward R. Lampson, Michael A. Ohi, Ryoma Mol Biol Cell Articles During cytokinesis, the chromosomal passenger complex (CPC) promotes midzone organization, specifies the cleavage plane, and regulates furrow contractility. The localizations of the CPC are coupled to its cytokinetic functions. At the metaphase-to-anaphase transition, the CPC dissociates from centromeres and localizes to midzone microtubules and the equatorial cortex. CPC relocalization to the cell middle is thought to depend on MKlp2-driven, plus end–directed transport. In support of this idea, MKlp2 depletion impairs cytokinesis; however, cytokinesis failure stems from furrow regression rather than failed initiation of furrowing. This suggests that an alternative mechanism(s) may concentrate the CPC at the division plane. We show here that direct actin binding, via the inner centromere protein (INCENP), enhances CPC enrichment at the equatorial cortex, thus acting in tandem with MKlp2. INCENP overexpression rescues furrowing in MKlp2-depleted cells in an INCENP-actin binding–dependent manner. Using live-cell imaging, we also find that MKlp2-dependent targeting of the CPC is biphasic. MKlp2 targets the CPC to the anti-parallel microtubule overlap of the midzone, after which the MKlp2-CPC complex moves in a nondirected manner. Collectively, our work suggests that both actin binding and MKlp2-dependent midzone targeting cooperate to precisely position the CPC during mitotic exit, and that these pathways converge to ensure successful cleavage furrow ingression. The American Society for Cell Biology 2017-12-01 /pmc/articles/PMC5706991/ /pubmed/28954866 http://dx.doi.org/10.1091/mbc.E17-06-0399 Text en © 2017 Landino et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Landino, Jennifer
Norris, Stephen R.
Li, Muyi
Ballister, Edward R.
Lampson, Michael A.
Ohi, Ryoma
Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title_full Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title_fullStr Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title_full_unstemmed Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title_short Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
title_sort two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5706991/
https://www.ncbi.nlm.nih.gov/pubmed/28954866
http://dx.doi.org/10.1091/mbc.E17-06-0399
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