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Supervillin binding to myosin II and synergism with anillin are required for cytokinesis
Cytokinesis, the process by which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking, and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II–binding proteins anillin...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842989/ https://www.ncbi.nlm.nih.gov/pubmed/24088567 http://dx.doi.org/10.1091/mbc.E12-10-0714 |
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author | Smith, Tara C. Fridy, Peter C. Li, Yinyin Basil, Shruti Arjun, Sneha Friesen, Ryan M. Leszyk, John Chait, Brian T. Rout, Michael P. Luna, Elizabeth J. |
author_facet | Smith, Tara C. Fridy, Peter C. Li, Yinyin Basil, Shruti Arjun, Sneha Friesen, Ryan M. Leszyk, John Chait, Brian T. Rout, Michael P. Luna, Elizabeth J. |
author_sort | Smith, Tara C. |
collection | PubMed |
description | Cytokinesis, the process by which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking, and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II–binding proteins anillin and supervillin, act earlier. Anillin's role in scaffolding the membrane cortex with the central spindle is well established, but the mechanism of supervillin action is relatively uncharacterized. We show here that two regions within supervillin affect cell division: residues 831–1281, which bind central spindle proteins, and residues 1–170, which bind the myosin II heavy chain (MHC) and the long form of myosin light-chain kinase. MHC binding is required to rescue supervillin deficiency, and mutagenesis of this site creates a dominant-negative phenotype. Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure. Knockdown of either protein causes mislocalization of the other, and endogenous anillin increases upon supervillin knockdown. Proteomic identification of interaction partners recovered using a high-affinity green fluorescent protein nanobody suggests that supervillin and anillin regulate the myosin II and actin cortical cytoskeletons through separate pathways. We conclude that supervillin and anillin play complementary roles during vertebrate cytokinesis. |
format | Online Article Text |
id | pubmed-3842989 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38429892014-02-16 Supervillin binding to myosin II and synergism with anillin are required for cytokinesis Smith, Tara C. Fridy, Peter C. Li, Yinyin Basil, Shruti Arjun, Sneha Friesen, Ryan M. Leszyk, John Chait, Brian T. Rout, Michael P. Luna, Elizabeth J. Mol Biol Cell Articles Cytokinesis, the process by which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking, and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II–binding proteins anillin and supervillin, act earlier. Anillin's role in scaffolding the membrane cortex with the central spindle is well established, but the mechanism of supervillin action is relatively uncharacterized. We show here that two regions within supervillin affect cell division: residues 831–1281, which bind central spindle proteins, and residues 1–170, which bind the myosin II heavy chain (MHC) and the long form of myosin light-chain kinase. MHC binding is required to rescue supervillin deficiency, and mutagenesis of this site creates a dominant-negative phenotype. Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure. Knockdown of either protein causes mislocalization of the other, and endogenous anillin increases upon supervillin knockdown. Proteomic identification of interaction partners recovered using a high-affinity green fluorescent protein nanobody suggests that supervillin and anillin regulate the myosin II and actin cortical cytoskeletons through separate pathways. We conclude that supervillin and anillin play complementary roles during vertebrate cytokinesis. The American Society for Cell Biology 2013-12-01 /pmc/articles/PMC3842989/ /pubmed/24088567 http://dx.doi.org/10.1091/mbc.E12-10-0714 Text en © 2013 Smith 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 of Cell Biology. |
spellingShingle | Articles Smith, Tara C. Fridy, Peter C. Li, Yinyin Basil, Shruti Arjun, Sneha Friesen, Ryan M. Leszyk, John Chait, Brian T. Rout, Michael P. Luna, Elizabeth J. Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title | Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title_full | Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title_fullStr | Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title_full_unstemmed | Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title_short | Supervillin binding to myosin II and synergism with anillin are required for cytokinesis |
title_sort | supervillin binding to myosin ii and synergism with anillin are required for cytokinesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842989/ https://www.ncbi.nlm.nih.gov/pubmed/24088567 http://dx.doi.org/10.1091/mbc.E12-10-0714 |
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