Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds?

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Cdc20 control of cell fate during prolonged mitotic arrest : do Cdc20 protein levels affect cell fate in response to antimitotic compounds? / Nilsson, Jakob.

In: BioEssays, Vol. 33, No. 12, 2011, p. 903-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nilsson, J 2011, 'Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds?', BioEssays, vol. 33, no. 12, pp. 903-9. https://doi.org/10.1002/bies.201100094

APA

Nilsson, J. (2011). Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds? BioEssays, 33(12), 903-9. https://doi.org/10.1002/bies.201100094

Vancouver

Nilsson J. Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds? BioEssays. 2011;33(12):903-9. https://doi.org/10.1002/bies.201100094

Author

Nilsson, Jakob. / Cdc20 control of cell fate during prolonged mitotic arrest : do Cdc20 protein levels affect cell fate in response to antimitotic compounds?. In: BioEssays. 2011 ; Vol. 33, No. 12. pp. 903-9.

Bibtex

@article{fb461fc1f42040218526342df5ecaa3a,
title = "Cdc20 control of cell fate during prolonged mitotic arrest: do Cdc20 protein levels affect cell fate in response to antimitotic compounds?",
abstract = "The fate of cells arrested in mitosis by antimitotic compounds is complex but is influenced by competition between pathways promoting cell death and pathways promoting mitotic exit. As components of both of these pathways are regulated by Cdc20-dependent degradation, I hypothesize that variations in Cdc20 protein levels, rather than mutations in checkpoint genes, could affect cell fate during prolonged mitotic arrest. This hypothesis is supported by experiments where manipulation of Cdc20 levels affects the response to antimitotic compounds. The observed differences in Cdc20 levels between cell lines likely reflects differences in the rate of synthesis or degradation of the protein; therefore, understanding these pathways at a molecular level could pave the way for modulating the activity of Cdc20, in turn presenting novel therapeutic possibilities.",
keywords = "Antimitotic Agents, Calcium-Binding Proteins, Cell Cycle Proteins, Cell Line, Cell Line, Tumor, Humans, M Phase Cell Cycle Checkpoints, Mitosis, Mutation, Phosphorylation, Protein-Serine-Threonine Kinases, Repressor Proteins",
author = "Jakob Nilsson",
note = "Copyright {\textcopyright} 2011 WILEY Periodicals, Inc.",
year = "2011",
doi = "10.1002/bies.201100094",
language = "English",
volume = "33",
pages = "903--9",
journal = "BioEssays",
issn = "0265-9247",
publisher = "Wiley",
number = "12",

}

RIS

TY - JOUR

T1 - Cdc20 control of cell fate during prolonged mitotic arrest

T2 - do Cdc20 protein levels affect cell fate in response to antimitotic compounds?

AU - Nilsson, Jakob

N1 - Copyright © 2011 WILEY Periodicals, Inc.

PY - 2011

Y1 - 2011

N2 - The fate of cells arrested in mitosis by antimitotic compounds is complex but is influenced by competition between pathways promoting cell death and pathways promoting mitotic exit. As components of both of these pathways are regulated by Cdc20-dependent degradation, I hypothesize that variations in Cdc20 protein levels, rather than mutations in checkpoint genes, could affect cell fate during prolonged mitotic arrest. This hypothesis is supported by experiments where manipulation of Cdc20 levels affects the response to antimitotic compounds. The observed differences in Cdc20 levels between cell lines likely reflects differences in the rate of synthesis or degradation of the protein; therefore, understanding these pathways at a molecular level could pave the way for modulating the activity of Cdc20, in turn presenting novel therapeutic possibilities.

AB - The fate of cells arrested in mitosis by antimitotic compounds is complex but is influenced by competition between pathways promoting cell death and pathways promoting mitotic exit. As components of both of these pathways are regulated by Cdc20-dependent degradation, I hypothesize that variations in Cdc20 protein levels, rather than mutations in checkpoint genes, could affect cell fate during prolonged mitotic arrest. This hypothesis is supported by experiments where manipulation of Cdc20 levels affects the response to antimitotic compounds. The observed differences in Cdc20 levels between cell lines likely reflects differences in the rate of synthesis or degradation of the protein; therefore, understanding these pathways at a molecular level could pave the way for modulating the activity of Cdc20, in turn presenting novel therapeutic possibilities.

KW - Antimitotic Agents

KW - Calcium-Binding Proteins

KW - Cell Cycle Proteins

KW - Cell Line

KW - Cell Line, Tumor

KW - Humans

KW - M Phase Cell Cycle Checkpoints

KW - Mitosis

KW - Mutation

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - Repressor Proteins

U2 - 10.1002/bies.201100094

DO - 10.1002/bies.201100094

M3 - Journal article

C2 - 22045620

VL - 33

SP - 903

EP - 909

JO - BioEssays

JF - BioEssays

SN - 0265-9247

IS - 12

ER -

ID: 40288994