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Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast

In fission yeast cells cortical nodes containing the protein Blt1p and several kinases appear early in G2, mature into cytokinetic nodes by adding anillin Mid1p, myosin-II, formin Cdc12p, and other proteins, and condense into a contractile ring by movements that depend on actin and myosin-II. Previo...

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Autores principales: Saha, Shambaditya, Pollard, Thomas D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469514/
https://www.ncbi.nlm.nih.gov/pubmed/22918943
http://dx.doi.org/10.1091/mbc.E12-07-0535
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author Saha, Shambaditya
Pollard, Thomas D.
author_facet Saha, Shambaditya
Pollard, Thomas D.
author_sort Saha, Shambaditya
collection PubMed
description In fission yeast cells cortical nodes containing the protein Blt1p and several kinases appear early in G2, mature into cytokinetic nodes by adding anillin Mid1p, myosin-II, formin Cdc12p, and other proteins, and condense into a contractile ring by movements that depend on actin and myosin-II. Previous studies concluded that cells without Mid1p lack cytokinetic nodes and assemble rings unreliably from myosin-II strands but left open questions. Why do strands form outside the equatorial region? Why is ring assembly unreliable without Mid1p? We found in Δmid1 cells that Cdc12p accumulates in cytokinetic nodes scattered in the cortex and produces actin filaments that associate with myosin-II, Rng2p, and Cdc15p to form strands located between the nodes. Strands incorporate nodes, and in ∼67% of cells, strands slowly close into rings that constrict without the normal ∼25-min maturation period. Ring assembly is unreliable and slow without Mid1p because the scattered Cdc12p nodes generate strands spread widely beyond the equator, and growing strands depend on random encounters to merge with other strands into a ring. We conclude that orderly assembly of the contractile ring in wild-type cells depends on Mid1p to recruit myosin-II, Rng2p, and Cdc15p to nodes and to place cytokinetic nodes around the cell equator.
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spelling pubmed-34695142012-12-30 Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast Saha, Shambaditya Pollard, Thomas D. Mol Biol Cell Articles In fission yeast cells cortical nodes containing the protein Blt1p and several kinases appear early in G2, mature into cytokinetic nodes by adding anillin Mid1p, myosin-II, formin Cdc12p, and other proteins, and condense into a contractile ring by movements that depend on actin and myosin-II. Previous studies concluded that cells without Mid1p lack cytokinetic nodes and assemble rings unreliably from myosin-II strands but left open questions. Why do strands form outside the equatorial region? Why is ring assembly unreliable without Mid1p? We found in Δmid1 cells that Cdc12p accumulates in cytokinetic nodes scattered in the cortex and produces actin filaments that associate with myosin-II, Rng2p, and Cdc15p to form strands located between the nodes. Strands incorporate nodes, and in ∼67% of cells, strands slowly close into rings that constrict without the normal ∼25-min maturation period. Ring assembly is unreliable and slow without Mid1p because the scattered Cdc12p nodes generate strands spread widely beyond the equator, and growing strands depend on random encounters to merge with other strands into a ring. We conclude that orderly assembly of the contractile ring in wild-type cells depends on Mid1p to recruit myosin-II, Rng2p, and Cdc15p to nodes and to place cytokinetic nodes around the cell equator. The American Society for Cell Biology 2012-10-15 /pmc/articles/PMC3469514/ /pubmed/22918943 http://dx.doi.org/10.1091/mbc.E12-07-0535 Text en © 2012 Saha and Pollard. 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 BD; are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Saha, Shambaditya
Pollard, Thomas D.
Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title_full Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title_fullStr Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title_full_unstemmed Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title_short Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
title_sort anillin-related protein mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469514/
https://www.ncbi.nlm.nih.gov/pubmed/22918943
http://dx.doi.org/10.1091/mbc.E12-07-0535
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