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Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast

In most cell types, mitosis and cytokinesis are tightly coupled such that cytokinesis occurs only once per cell cycle. The fission yeast Schizosaccharomyces pombe divides using an actomyosin-based contractile ring and is an attractive model for the study of the links between mitosis and cytokinesis....

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Autores principales: Chew, Ting Gang, Balasubramanian, Mohan K
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213707/
https://www.ncbi.nlm.nih.gov/pubmed/18225957
http://dx.doi.org/10.1371/journal.pgen.0040017
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author Chew, Ting Gang
Balasubramanian, Mohan K
author_facet Chew, Ting Gang
Balasubramanian, Mohan K
author_sort Chew, Ting Gang
collection PubMed
description In most cell types, mitosis and cytokinesis are tightly coupled such that cytokinesis occurs only once per cell cycle. The fission yeast Schizosaccharomyces pombe divides using an actomyosin-based contractile ring and is an attractive model for the study of the links between mitosis and cytokinesis. In fission yeast, the anaphase-promoting complex/cyclosome (APC/C) and the septation initiation network (SIN), a spindle pole body (SPB)–associated GTPase-driven signaling cascade, function sequentially to ensure proper coordination of mitosis and cytokinesis. Here, we find a novel interplay between the tetratricopeptide repeat (TPR) domain–containing subunit of the APC/C, Nuc2p, and the SIN, that appears to not involve other subunits of the APC/C. Overproduction of Nuc2p led to an increase in the presence of multinucleated cells, which correlated with a defect in actomyosin ring maintenance and localization of the SIN component protein kinases Cdc7p and Sid1p to the SPBs, indicative of defective SIN signaling. Conversely, loss of Nuc2p function led to increased SIN signaling, characterized by the persistent localization of Cdc7p and Sid1p on SPBs and assembly of multiple actomyosin rings and division septa. Nuc2p appears to function independently of the checkpoint with FHA and ring finger (CHFR)–related protein Dma1p, a known inhibitor of the SIN in fission yeast. Genetic and biochemical analyses established that Nuc2p might influence the nucleotide state of Spg1p GTPase, a key regulator of the SIN. We propose that Nuc2p, by inhibiting the SIN after cell division, prevents further deleterious cytokinetic events, thereby contributing to genome stability.
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spelling pubmed-22137072008-01-25 Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast Chew, Ting Gang Balasubramanian, Mohan K PLoS Genet Research Article In most cell types, mitosis and cytokinesis are tightly coupled such that cytokinesis occurs only once per cell cycle. The fission yeast Schizosaccharomyces pombe divides using an actomyosin-based contractile ring and is an attractive model for the study of the links between mitosis and cytokinesis. In fission yeast, the anaphase-promoting complex/cyclosome (APC/C) and the septation initiation network (SIN), a spindle pole body (SPB)–associated GTPase-driven signaling cascade, function sequentially to ensure proper coordination of mitosis and cytokinesis. Here, we find a novel interplay between the tetratricopeptide repeat (TPR) domain–containing subunit of the APC/C, Nuc2p, and the SIN, that appears to not involve other subunits of the APC/C. Overproduction of Nuc2p led to an increase in the presence of multinucleated cells, which correlated with a defect in actomyosin ring maintenance and localization of the SIN component protein kinases Cdc7p and Sid1p to the SPBs, indicative of defective SIN signaling. Conversely, loss of Nuc2p function led to increased SIN signaling, characterized by the persistent localization of Cdc7p and Sid1p on SPBs and assembly of multiple actomyosin rings and division septa. Nuc2p appears to function independently of the checkpoint with FHA and ring finger (CHFR)–related protein Dma1p, a known inhibitor of the SIN in fission yeast. Genetic and biochemical analyses established that Nuc2p might influence the nucleotide state of Spg1p GTPase, a key regulator of the SIN. We propose that Nuc2p, by inhibiting the SIN after cell division, prevents further deleterious cytokinetic events, thereby contributing to genome stability. Public Library of Science 2008-01 2008-01-25 /pmc/articles/PMC2213707/ /pubmed/18225957 http://dx.doi.org/10.1371/journal.pgen.0040017 Text en © 2008 Chew and Balasubramanian. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Chew, Ting Gang
Balasubramanian, Mohan K
Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title_full Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title_fullStr Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title_full_unstemmed Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title_short Nuc2p, a Subunit of the Anaphase-Promoting Complex, Inhibits Septation Initiation Network Following Cytokinesis in Fission Yeast
title_sort nuc2p, a subunit of the anaphase-promoting complex, inhibits septation initiation network following cytokinesis in fission yeast
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213707/
https://www.ncbi.nlm.nih.gov/pubmed/18225957
http://dx.doi.org/10.1371/journal.pgen.0040017
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