Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis

Yves Matthess; Monika Raab; Rainald Knecht; Sven Becker; Klaus Strebhardt

doi:10.1016/j.molonc.2013.12.013

Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis

Standard

Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis. / Matthess, Yves; Raab, Monika; Knecht, Rainald; Becker, Sven; Strebhardt, Klaus.

In: MOL ONCOL, Vol. 8, No. 3, 2014, p. 596-608.

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

Harvard

Matthess, Y, Raab, M, Knecht, R, Becker, S & Strebhardt, K 2014, 'Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis', MOL ONCOL, vol. 8, no. 3, pp. 596-608. https://doi.org/10.1016/j.molonc.2013.12.013

APA

Matthess, Y., Raab, M., Knecht, R., Becker, S., & Strebhardt, K. (2014). Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis. MOL ONCOL, 8(3), 596-608. https://doi.org/10.1016/j.molonc.2013.12.013

Vancouver

Matthess Y, Raab M, Knecht R, Becker S, Strebhardt K. Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis. MOL ONCOL. 2014;8(3):596-608. https://doi.org/10.1016/j.molonc.2013.12.013

Bibtex

@article{a18f42d0e33743999d685526a8f62fb2,

title = "Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis",

abstract = "Caspase-8 is crucial for cell death induction, especially via the death receptor pathway. The dysregulated expression or function of caspase-8 can promote tumor formation, progression and treatment resistance in different human cancers. Here, we show procaspase-8 is regulated during the cell cycle through the concerted inhibitory action of Cdk1/cyclin B1 and polo-like kinase 1 (Plk1). By phosphorylating S387 in procaspase-8 Cdk1/cyclin B1 generates a phospho-epitope for the binding of the PBD of Plk1. Subsequently, S305 in procaspase-8 is phosphorylated by Plk1 during mitosis. Using an RNAi-based strategy we could demonstrate that the extrinsic cell death is increased upon Fas-stimulation when endogenous caspase-8 is replaced by a mutant (S305A) mimicking the non-phosphorylated form. Together, our data show that sequential phosphorylation by Cdk1/cyclin B1 and Plk1 decreases the sensitivity of cells toward stimuli of the extrinsic pathway during mitosis. Thus, the clinical Plk1 inhibitor BI 2536 decreases the threshold of different cancer cell types toward Fas-induced cell death.",

keywords = "Apoptosis, Caspase 8, Cell Cycle, Cell Cycle Proteins, Cyclin-Dependent Kinases, HeLa Cells, Humans, Mitosis, Mutation, Neoplasms, Phosphorylation, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins",

author = "Yves Matthess and Monika Raab and Rainald Knecht and Sven Becker and Klaus Strebhardt",

year = "2014",

doi = "10.1016/j.molonc.2013.12.013",

language = "English",

volume = "8",

pages = "596--608",

journal = "MOL ONCOL",

issn = "1574-7891",

publisher = "Elsevier",

number = "3",

}

RIS

TY - JOUR

T1 - Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis

AU - Matthess, Yves

AU - Raab, Monika

AU - Knecht, Rainald

AU - Becker, Sven

AU - Strebhardt, Klaus

PY - 2014

Y1 - 2014

N2 - Caspase-8 is crucial for cell death induction, especially via the death receptor pathway. The dysregulated expression or function of caspase-8 can promote tumor formation, progression and treatment resistance in different human cancers. Here, we show procaspase-8 is regulated during the cell cycle through the concerted inhibitory action of Cdk1/cyclin B1 and polo-like kinase 1 (Plk1). By phosphorylating S387 in procaspase-8 Cdk1/cyclin B1 generates a phospho-epitope for the binding of the PBD of Plk1. Subsequently, S305 in procaspase-8 is phosphorylated by Plk1 during mitosis. Using an RNAi-based strategy we could demonstrate that the extrinsic cell death is increased upon Fas-stimulation when endogenous caspase-8 is replaced by a mutant (S305A) mimicking the non-phosphorylated form. Together, our data show that sequential phosphorylation by Cdk1/cyclin B1 and Plk1 decreases the sensitivity of cells toward stimuli of the extrinsic pathway during mitosis. Thus, the clinical Plk1 inhibitor BI 2536 decreases the threshold of different cancer cell types toward Fas-induced cell death.

AB - Caspase-8 is crucial for cell death induction, especially via the death receptor pathway. The dysregulated expression or function of caspase-8 can promote tumor formation, progression and treatment resistance in different human cancers. Here, we show procaspase-8 is regulated during the cell cycle through the concerted inhibitory action of Cdk1/cyclin B1 and polo-like kinase 1 (Plk1). By phosphorylating S387 in procaspase-8 Cdk1/cyclin B1 generates a phospho-epitope for the binding of the PBD of Plk1. Subsequently, S305 in procaspase-8 is phosphorylated by Plk1 during mitosis. Using an RNAi-based strategy we could demonstrate that the extrinsic cell death is increased upon Fas-stimulation when endogenous caspase-8 is replaced by a mutant (S305A) mimicking the non-phosphorylated form. Together, our data show that sequential phosphorylation by Cdk1/cyclin B1 and Plk1 decreases the sensitivity of cells toward stimuli of the extrinsic pathway during mitosis. Thus, the clinical Plk1 inhibitor BI 2536 decreases the threshold of different cancer cell types toward Fas-induced cell death.

KW - Apoptosis

KW - Caspase 8

KW - Cell Cycle

KW - Cell Cycle Proteins

KW - Cyclin-Dependent Kinases

KW - HeLa Cells

KW - Humans

KW - Mitosis

KW - Mutation

KW - Neoplasms

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - Proto-Oncogene Proteins

U2 - 10.1016/j.molonc.2013.12.013

DO - 10.1016/j.molonc.2013.12.013

M3 - SCORING: Journal article

C2 - 24484936

VL - 8

SP - 596

EP - 608

JO - MOL ONCOL

JF - MOL ONCOL

SN - 1574-7891

IS - 3

ER -