New insights into the cellular temporal response to proteostatic stress

Justin Rendleman; Zhe Cheng; Shuvadeep Maity; Nicolai Kastelic; Mathias Munschauer; Kristina Allgoewer; Guoshou Teo; Yun Bin Matteo Zhang; Amy Lei; Brian Parker; Markus Landthaler; Lindsay Freeberg; Scott Kuersten; Hyungwon Choi; Christine Vogel

doi:10.7554/eLife.39054

New insights into the cellular temporal response to proteostatic stress

Standard

New insights into the cellular temporal response to proteostatic stress. / Rendleman, Justin; Cheng, Zhe; Maity, Shuvadeep; Kastelic, Nicolai; Munschauer, Mathias; Allgoewer, Kristina; Teo, Guoshou; Zhang, Yun Bin Matteo; Lei, Amy; Parker, Brian; Landthaler, Markus; Freeberg, Lindsay; Kuersten, Scott; Choi, Hyungwon; Vogel, Christine.

in: ELIFE, Jahrgang 7, 12.10.2018, S. e39054.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Rendleman, J, Cheng, Z, Maity, S, Kastelic, N, Munschauer, M, Allgoewer, K, Teo, G, Zhang, YBM, Lei, A, Parker, B, Landthaler, M, Freeberg, L, Kuersten, S, Choi, H & Vogel, C 2018, 'New insights into the cellular temporal response to proteostatic stress', ELIFE, Jg. 7, S. e39054. https://doi.org/10.7554/eLife.39054

APA

Rendleman, J., Cheng, Z., Maity, S., Kastelic, N., Munschauer, M., Allgoewer, K., Teo, G., Zhang, Y. B. M., Lei, A., Parker, B., Landthaler, M., Freeberg, L., Kuersten, S., Choi, H., & Vogel, C. (2018). New insights into the cellular temporal response to proteostatic stress. ELIFE, 7, e39054. https://doi.org/10.7554/eLife.39054

Vancouver

Rendleman J, Cheng Z, Maity S, Kastelic N, Munschauer M, Allgoewer K et al. New insights into the cellular temporal response to proteostatic stress. ELIFE. 2018 Okt 12;7:e39054. https://doi.org/10.7554/eLife.39054

Bibtex

@article{6cbfdab851964589aff5b84b777c5c3e,

title = "New insights into the cellular temporal response to proteostatic stress",

abstract = "Maintaining a healthy proteome involves all layers of gene expression regulation. By quantifying temporal changes of the transcriptome, translatome, proteome, and RNA-protein interactome in cervical cancer cells, we systematically characterize the molecular landscape in response to proteostatic challenges. We identify shared and specific responses to misfolded proteins and to oxidative stress, two conditions that are tightly linked. We reveal new aspects of the unfolded protein response, including many genes that escape global translation shutdown. A subset of these genes supports rerouting of energy production in the mitochondria. We also find that many genes change at multiple levels, in either the same or opposing directions, and at different time points. We highlight a variety of putative regulatory pathways, including the stress-dependent alternative splicing of aminoacyl-tRNA synthetases, and protein-RNA binding within the 3' untranslated region of molecular chaperones. These results illustrate the potential of this information-rich resource.",

keywords = "Amino Acyl-tRNA Synthetases/metabolism, DNA Repair/genetics, Endoplasmic Reticulum/drug effects, Endoplasmic Reticulum Stress/drug effects, Eukaryotic Initiation Factor-2/metabolism, Gene Expression Regulation/drug effects, Genes, Essential, HeLa Cells, Humans, Membrane Proteins/metabolism, Nucleic Acid Conformation, Open Reading Frames/genetics, Principal Component Analysis, Protein Biosynthesis/drug effects, Proteostasis/drug effects, Ribosomes/drug effects, Signal Transduction/drug effects, Stress, Physiological/drug effects, Time Factors, Transcription, Genetic/drug effects, Tunicamycin/pharmacology, Unfolded Protein Response/drug effects, eIF-2 Kinase/metabolism",

author = "Justin Rendleman and Zhe Cheng and Shuvadeep Maity and Nicolai Kastelic and Mathias Munschauer and Kristina Allgoewer and Guoshou Teo and Zhang, {Yun Bin Matteo} and Amy Lei and Brian Parker and Markus Landthaler and Lindsay Freeberg and Scott Kuersten and Hyungwon Choi and Christine Vogel",

note = "{\textcopyright} 2018, Rendleman et al.",

year = "2018",

month = oct,

day = "12",

doi = "10.7554/eLife.39054",

language = "English",

volume = "7",

pages = "e39054",

journal = "ELIFE",

issn = "2050-084X",

publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - New insights into the cellular temporal response to proteostatic stress

AU - Rendleman, Justin

AU - Cheng, Zhe

AU - Maity, Shuvadeep

AU - Kastelic, Nicolai

AU - Munschauer, Mathias

AU - Allgoewer, Kristina

AU - Teo, Guoshou

AU - Zhang, Yun Bin Matteo

AU - Lei, Amy

AU - Parker, Brian

AU - Landthaler, Markus

AU - Freeberg, Lindsay

AU - Kuersten, Scott

AU - Choi, Hyungwon

AU - Vogel, Christine

PY - 2018/10/12

Y1 - 2018/10/12

N2 - Maintaining a healthy proteome involves all layers of gene expression regulation. By quantifying temporal changes of the transcriptome, translatome, proteome, and RNA-protein interactome in cervical cancer cells, we systematically characterize the molecular landscape in response to proteostatic challenges. We identify shared and specific responses to misfolded proteins and to oxidative stress, two conditions that are tightly linked. We reveal new aspects of the unfolded protein response, including many genes that escape global translation shutdown. A subset of these genes supports rerouting of energy production in the mitochondria. We also find that many genes change at multiple levels, in either the same or opposing directions, and at different time points. We highlight a variety of putative regulatory pathways, including the stress-dependent alternative splicing of aminoacyl-tRNA synthetases, and protein-RNA binding within the 3' untranslated region of molecular chaperones. These results illustrate the potential of this information-rich resource.

AB - Maintaining a healthy proteome involves all layers of gene expression regulation. By quantifying temporal changes of the transcriptome, translatome, proteome, and RNA-protein interactome in cervical cancer cells, we systematically characterize the molecular landscape in response to proteostatic challenges. We identify shared and specific responses to misfolded proteins and to oxidative stress, two conditions that are tightly linked. We reveal new aspects of the unfolded protein response, including many genes that escape global translation shutdown. A subset of these genes supports rerouting of energy production in the mitochondria. We also find that many genes change at multiple levels, in either the same or opposing directions, and at different time points. We highlight a variety of putative regulatory pathways, including the stress-dependent alternative splicing of aminoacyl-tRNA synthetases, and protein-RNA binding within the 3' untranslated region of molecular chaperones. These results illustrate the potential of this information-rich resource.

KW - Amino Acyl-tRNA Synthetases/metabolism

KW - DNA Repair/genetics

KW - Endoplasmic Reticulum/drug effects

KW - Endoplasmic Reticulum Stress/drug effects

KW - Eukaryotic Initiation Factor-2/metabolism

KW - Gene Expression Regulation/drug effects

KW - Genes, Essential

KW - HeLa Cells

KW - Humans

KW - Membrane Proteins/metabolism

KW - Nucleic Acid Conformation

KW - Open Reading Frames/genetics

KW - Principal Component Analysis

KW - Protein Biosynthesis/drug effects

KW - Proteostasis/drug effects

KW - Ribosomes/drug effects

KW - Signal Transduction/drug effects

KW - Stress, Physiological/drug effects

KW - Time Factors

KW - Transcription, Genetic/drug effects

KW - Tunicamycin/pharmacology

KW - Unfolded Protein Response/drug effects

KW - eIF-2 Kinase/metabolism

U2 - 10.7554/eLife.39054

DO - 10.7554/eLife.39054

M3 - SCORING: Journal article

C2 - 30272558

VL - 7

SP - e39054

JO - ELIFE

JF - ELIFE

SN - 2050-084X

ER -