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Characterization of the roles of Blt1p in fission yeast cytokinesis

Spatial and temporal regulation of cytokinesis is essential for cell division, yet the mechanisms that control the formation and constriction of the contractile ring are incompletely understood. In the fission yeast Schizosaccharomyces pombe proteins that contribute to the cytokinetic contractile ri...

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Autores principales: Goss, John W., Kim, Sunhee, Bledsoe, Hannah, Pollard, Thomas D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4072569/
https://www.ncbi.nlm.nih.gov/pubmed/24790095
http://dx.doi.org/10.1091/mbc.E13-06-0300
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author Goss, John W.
Kim, Sunhee
Bledsoe, Hannah
Pollard, Thomas D.
author_facet Goss, John W.
Kim, Sunhee
Bledsoe, Hannah
Pollard, Thomas D.
author_sort Goss, John W.
collection PubMed
description Spatial and temporal regulation of cytokinesis is essential for cell division, yet the mechanisms that control the formation and constriction of the contractile ring are incompletely understood. In the fission yeast Schizosaccharomyces pombe proteins that contribute to the cytokinetic contractile ring accumulate during interphase in nodes—precursor structures around the equatorial cortex. During mitosis, additional proteins join these nodes, which condense to form the contractile ring. The cytokinesis protein Blt1p is unique in being present continuously in nodes from early interphase through to the contractile ring until cell separation. Blt1p was shown to stabilize interphase nodes, but its functions later in mitosis were unclear. We use analytical ultracentrifugation to show that purified Blt1p is a tetramer. We find that Blt1p interacts physically with Sid2p and Mob1p, a protein kinase complex of the septation initiation network, and confirm known interactions with F-BAR protein Cdc15p. Contractile rings assemble normally in blt1∆ cells, but the initiation of ring constriction and completion of cell division are delayed. We find three defects that likely contribute to this delay. Without Blt1p, contractile rings recruited and retained less Sid2p/Mob1p and Clp1p phosphatase, and β-glucan synthase Bgs1p accumulated slowly at the cleavage site.
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spelling pubmed-40725692014-09-16 Characterization of the roles of Blt1p in fission yeast cytokinesis Goss, John W. Kim, Sunhee Bledsoe, Hannah Pollard, Thomas D. Mol Biol Cell Articles Spatial and temporal regulation of cytokinesis is essential for cell division, yet the mechanisms that control the formation and constriction of the contractile ring are incompletely understood. In the fission yeast Schizosaccharomyces pombe proteins that contribute to the cytokinetic contractile ring accumulate during interphase in nodes—precursor structures around the equatorial cortex. During mitosis, additional proteins join these nodes, which condense to form the contractile ring. The cytokinesis protein Blt1p is unique in being present continuously in nodes from early interphase through to the contractile ring until cell separation. Blt1p was shown to stabilize interphase nodes, but its functions later in mitosis were unclear. We use analytical ultracentrifugation to show that purified Blt1p is a tetramer. We find that Blt1p interacts physically with Sid2p and Mob1p, a protein kinase complex of the septation initiation network, and confirm known interactions with F-BAR protein Cdc15p. Contractile rings assemble normally in blt1∆ cells, but the initiation of ring constriction and completion of cell division are delayed. We find three defects that likely contribute to this delay. Without Blt1p, contractile rings recruited and retained less Sid2p/Mob1p and Clp1p phosphatase, and β-glucan synthase Bgs1p accumulated slowly at the cleavage site. The American Society for Cell Biology 2014-07-01 /pmc/articles/PMC4072569/ /pubmed/24790095 http://dx.doi.org/10.1091/mbc.E13-06-0300 Text en © 2014 Goss 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
Goss, John W.
Kim, Sunhee
Bledsoe, Hannah
Pollard, Thomas D.
Characterization of the roles of Blt1p in fission yeast cytokinesis
title Characterization of the roles of Blt1p in fission yeast cytokinesis
title_full Characterization of the roles of Blt1p in fission yeast cytokinesis
title_fullStr Characterization of the roles of Blt1p in fission yeast cytokinesis
title_full_unstemmed Characterization of the roles of Blt1p in fission yeast cytokinesis
title_short Characterization of the roles of Blt1p in fission yeast cytokinesis
title_sort characterization of the roles of blt1p in fission yeast cytokinesis
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4072569/
https://www.ncbi.nlm.nih.gov/pubmed/24790095
http://dx.doi.org/10.1091/mbc.E13-06-0300
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