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Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle

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Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle. / Chiu, Hung-Chuan; Huang, Wei-Ru; Liao, Tsai-Ling et al.
In: PLoS ONE, Vol. 11, No. 9, e0162356, 07.09.2016.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Chiu, H-C, Huang, W-R, Liao, T-L, Wu, H-Y, Munir, M, Shih, W-L & Liu, H-J 2016, 'Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle', PLoS ONE, vol. 11, no. 9, e0162356. https://doi.org/10.1371/journal.pone.0162356

APA

Chiu, H-C., Huang, W-R., Liao, T-L., Wu, H-Y., Munir, M., Shih, W-L., & Liu, H-J. (2016). Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle. PLoS ONE, 11(9), Article e0162356. https://doi.org/10.1371/journal.pone.0162356

Vancouver

Chiu H-C, Huang W-R, Liao T-L, Wu H-Y, Munir M, Shih W-L et al. Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle. PLoS ONE. 2016 Sept 7;11(9):e0162356. doi: 10.1371/journal.pone.0162356

Author

Chiu, Hung-Chuan ; Huang, Wei-Ru ; Liao, Tsai-Ling et al. / Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle. In: PLoS ONE. 2016 ; Vol. 11, No. 9.

Bibtex

@article{948d8a298b1c4649889be59522a3c4f0,
title = "Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle",
abstract = "The p17 protein of avian reovirus (ARV) causes cell cycle retardation in a variety of cell lines; however, the underlying mechanism(s) by which p17 regulates the cell cycle remains largely unknown. We demonstrate for the first time that p17 interacts with CDK1 and vimentin as revealed by reciprocal co-immunoprecipitation and GST pull-down assays. Both in vitro and in vivo studies indicated that direct interaction of p17 and CDK1/vimentin was mapped within the amino terminus (aa 1-60) of p17 and central region (aa 27-118) of CDK1/vimentin. Furthermore, p17 was found to occupy the Plk1-binding site within the vimentin, thereby blocking Plk1 recruitment to CDK1-induced vimentin phosphorylation at Ser 56. Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Furthermore, we have identified upstream signaling pathways and cellular factor(s) targeted by p17 and found that p17 regulates inhibitory phosphorylation of CDK1 and blocks vimentin phosphorylation at Ser 56 and Ser 82. The p17-mediated inactivation of CDK1 is dependent on several mechanisms, which include direct interaction with CDK1, p17-mediated suppression of Plk1 by activating the Tpr/p53 and ATM/Chk1/PP2A pathways, and p17-mediated cdc25C degradation via an ubiquitin- proteasome pathway. Additionally, depletion of p53 with a shRNA as well as inhibition of ATM and vimentin by inhibitors diminished virus yield while Tpr and CDK1 knockdown increased virus yield. Taken together, results demonstrate that p17 suppresses both CDK1 and Plk1functions, disrupts vimentin phosphorylation, causes G2/M cell cycle arrest and thus benefits virus replication.",
keywords = "Animals, Ataxia Telangiectasia Mutated Proteins, CDC2 Protein Kinase, Cell Cycle Proteins, Cell Division, Cell Proliferation, Cercopithecus aethiops, Checkpoint Kinase 1, Chick Embryo, Cyclin-Dependent Kinase Inhibitor p21, Down-Regulation, G2 Phase, Immunoprecipitation, Models, Biological, Nuclear Pore Complex Proteins, Orthoreovirus, Avian, Phosphorylation, Phosphoserine, Proteasome Endopeptidase Complex, Protein Binding, Protein Interaction Domains and Motifs, Protein-Serine-Threonine Kinases, Proteolysis, Proto-Oncogene Proteins, Signal Transduction, Transfection, Tumor Suppressor Protein p53, Ubiquitin, Up-Regulation, Vero Cells, Vimentin, Viral Proteins, Virus Replication, cdc25 Phosphatases, Journal Article",
author = "Hung-Chuan Chiu and Wei-Ru Huang and Tsai-Ling Liao and Hung-Yi Wu and Muhammad Munir and Wing-Ling Shih and Hung-Jen Liu",
year = "2016",
month = sep,
day = "7",
doi = "10.1371/journal.pone.0162356",
language = "English",
volume = "11",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "9",

}

RIS

TY - JOUR

T1 - Suppression of Vimentin Phosphorylation by the Avian Reovirus p17 through Inhibition of CDK1 and Plk1 Impacting the G2/M Phase of the Cell Cycle

AU - Chiu, Hung-Chuan

AU - Huang, Wei-Ru

AU - Liao, Tsai-Ling

AU - Wu, Hung-Yi

AU - Munir, Muhammad

AU - Shih, Wing-Ling

AU - Liu, Hung-Jen

PY - 2016/9/7

Y1 - 2016/9/7

N2 - The p17 protein of avian reovirus (ARV) causes cell cycle retardation in a variety of cell lines; however, the underlying mechanism(s) by which p17 regulates the cell cycle remains largely unknown. We demonstrate for the first time that p17 interacts with CDK1 and vimentin as revealed by reciprocal co-immunoprecipitation and GST pull-down assays. Both in vitro and in vivo studies indicated that direct interaction of p17 and CDK1/vimentin was mapped within the amino terminus (aa 1-60) of p17 and central region (aa 27-118) of CDK1/vimentin. Furthermore, p17 was found to occupy the Plk1-binding site within the vimentin, thereby blocking Plk1 recruitment to CDK1-induced vimentin phosphorylation at Ser 56. Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Furthermore, we have identified upstream signaling pathways and cellular factor(s) targeted by p17 and found that p17 regulates inhibitory phosphorylation of CDK1 and blocks vimentin phosphorylation at Ser 56 and Ser 82. The p17-mediated inactivation of CDK1 is dependent on several mechanisms, which include direct interaction with CDK1, p17-mediated suppression of Plk1 by activating the Tpr/p53 and ATM/Chk1/PP2A pathways, and p17-mediated cdc25C degradation via an ubiquitin- proteasome pathway. Additionally, depletion of p53 with a shRNA as well as inhibition of ATM and vimentin by inhibitors diminished virus yield while Tpr and CDK1 knockdown increased virus yield. Taken together, results demonstrate that p17 suppresses both CDK1 and Plk1functions, disrupts vimentin phosphorylation, causes G2/M cell cycle arrest and thus benefits virus replication.

AB - The p17 protein of avian reovirus (ARV) causes cell cycle retardation in a variety of cell lines; however, the underlying mechanism(s) by which p17 regulates the cell cycle remains largely unknown. We demonstrate for the first time that p17 interacts with CDK1 and vimentin as revealed by reciprocal co-immunoprecipitation and GST pull-down assays. Both in vitro and in vivo studies indicated that direct interaction of p17 and CDK1/vimentin was mapped within the amino terminus (aa 1-60) of p17 and central region (aa 27-118) of CDK1/vimentin. Furthermore, p17 was found to occupy the Plk1-binding site within the vimentin, thereby blocking Plk1 recruitment to CDK1-induced vimentin phosphorylation at Ser 56. Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Furthermore, we have identified upstream signaling pathways and cellular factor(s) targeted by p17 and found that p17 regulates inhibitory phosphorylation of CDK1 and blocks vimentin phosphorylation at Ser 56 and Ser 82. The p17-mediated inactivation of CDK1 is dependent on several mechanisms, which include direct interaction with CDK1, p17-mediated suppression of Plk1 by activating the Tpr/p53 and ATM/Chk1/PP2A pathways, and p17-mediated cdc25C degradation via an ubiquitin- proteasome pathway. Additionally, depletion of p53 with a shRNA as well as inhibition of ATM and vimentin by inhibitors diminished virus yield while Tpr and CDK1 knockdown increased virus yield. Taken together, results demonstrate that p17 suppresses both CDK1 and Plk1functions, disrupts vimentin phosphorylation, causes G2/M cell cycle arrest and thus benefits virus replication.

KW - Animals

KW - Ataxia Telangiectasia Mutated Proteins

KW - CDC2 Protein Kinase

KW - Cell Cycle Proteins

KW - Cell Division

KW - Cell Proliferation

KW - Cercopithecus aethiops

KW - Checkpoint Kinase 1

KW - Chick Embryo

KW - Cyclin-Dependent Kinase Inhibitor p21

KW - Down-Regulation

KW - G2 Phase

KW - Immunoprecipitation

KW - Models, Biological

KW - Nuclear Pore Complex Proteins

KW - Orthoreovirus, Avian

KW - Phosphorylation

KW - Phosphoserine

KW - Proteasome Endopeptidase Complex

KW - Protein Binding

KW - Protein Interaction Domains and Motifs

KW - Protein-Serine-Threonine Kinases

KW - Proteolysis

KW - Proto-Oncogene Proteins

KW - Signal Transduction

KW - Transfection

KW - Tumor Suppressor Protein p53

KW - Ubiquitin

KW - Up-Regulation

KW - Vero Cells

KW - Vimentin

KW - Viral Proteins

KW - Virus Replication

KW - cdc25 Phosphatases

KW - Journal Article

U2 - 10.1371/journal.pone.0162356

DO - 10.1371/journal.pone.0162356

M3 - Journal article

C2 - 27603133

VL - 11

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 9

M1 - e0162356

ER -