Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress

Here, we present quantitative subcellular compartment-specific proteomic data from wildtype and DYT-TOR1A heterozygous mouse embryonic fibroblasts (MEFs) basally and following thapsigargin (Tg) treatment [1]. In this experiment, we generated MEFs from wild type (WT) and a heterozygous DYT-TOR1A mous...

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Autores principales: Kunal Shroff, Zachary F. Caffall, Erik J. Soderblom, Greg Waitt, Tricia Ho, Nicole Calakos
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Lenguaje:EN
Publicado: Elsevier 2021
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Acceso en línea:https://doaj.org/article/92b04d4359d04b72a79daef5697143b3
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spelling oai:doaj.org-article:92b04d4359d04b72a79daef5697143b32021-12-02T05:01:50ZDataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress2352-340910.1016/j.dib.2021.107609https://doaj.org/article/92b04d4359d04b72a79daef5697143b32021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2352340921008842https://doaj.org/toc/2352-3409Here, we present quantitative subcellular compartment-specific proteomic data from wildtype and DYT-TOR1A heterozygous mouse embryonic fibroblasts (MEFs) basally and following thapsigargin (Tg) treatment [1]. In this experiment, we generated MEFs from wild type (WT) and a heterozygous DYT-TOR1A mouse model of dystonia. Subsequently, these MEF cultures were treated with either 1 µM Tg or dimethylsulfoxide vehicle (Veh) for six hours. Following treatment, the cells were fractionated into nuclear and cytosolic fractions. Liquid chromatography, tandem mass spectrometry (LC/MS/MS)-based proteomic profiling identified 65,056 unique peptides and 4801 unique proteins across all samples. The data presented here provide subcellular compartment-specific proteomic information within a dystonia model system both basally and under cellular stress. These data can inform future experiments focused on studying the function of TorsinA, the protein encoded by TOR1A, and its potential role in nucleocytoplasmic transport and proteostasis. In addition, the information in this article can also inform future mechanistic studies investigating the relationship between DYT-TOR1A dystonia and the cellular stress response to advance understanding of the pathogenesis of dystonia.Kunal ShroffZachary F. CaffallErik J. SoderblomGreg WaittTricia HoNicole CalakosElsevierarticleDystoniaTorsinAProteomicsSubcellular fractionationThapsigarginStress responseComputer applications to medicine. Medical informaticsR858-859.7Science (General)Q1-390ENData in Brief, Vol 39, Iss , Pp 107609- (2021)
institution DOAJ
collection DOAJ
language EN
topic Dystonia
TorsinA
Proteomics
Subcellular fractionation
Thapsigargin
Stress response
Computer applications to medicine. Medical informatics
R858-859.7
Science (General)
Q1-390
spellingShingle Dystonia
TorsinA
Proteomics
Subcellular fractionation
Thapsigargin
Stress response
Computer applications to medicine. Medical informatics
R858-859.7
Science (General)
Q1-390
Kunal Shroff
Zachary F. Caffall
Erik J. Soderblom
Greg Waitt
Tricia Ho
Nicole Calakos
Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
description Here, we present quantitative subcellular compartment-specific proteomic data from wildtype and DYT-TOR1A heterozygous mouse embryonic fibroblasts (MEFs) basally and following thapsigargin (Tg) treatment [1]. In this experiment, we generated MEFs from wild type (WT) and a heterozygous DYT-TOR1A mouse model of dystonia. Subsequently, these MEF cultures were treated with either 1 µM Tg or dimethylsulfoxide vehicle (Veh) for six hours. Following treatment, the cells were fractionated into nuclear and cytosolic fractions. Liquid chromatography, tandem mass spectrometry (LC/MS/MS)-based proteomic profiling identified 65,056 unique peptides and 4801 unique proteins across all samples. The data presented here provide subcellular compartment-specific proteomic information within a dystonia model system both basally and under cellular stress. These data can inform future experiments focused on studying the function of TorsinA, the protein encoded by TOR1A, and its potential role in nucleocytoplasmic transport and proteostasis. In addition, the information in this article can also inform future mechanistic studies investigating the relationship between DYT-TOR1A dystonia and the cellular stress response to advance understanding of the pathogenesis of dystonia.
format article
author Kunal Shroff
Zachary F. Caffall
Erik J. Soderblom
Greg Waitt
Tricia Ho
Nicole Calakos
author_facet Kunal Shroff
Zachary F. Caffall
Erik J. Soderblom
Greg Waitt
Tricia Ho
Nicole Calakos
author_sort Kunal Shroff
title Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
title_short Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
title_full Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
title_fullStr Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
title_full_unstemmed Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress
title_sort dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and dyt-tor1a mouse model of dystonia, basally and during stress
publisher Elsevier
publishDate 2021
url https://doaj.org/article/92b04d4359d04b72a79daef5697143b3
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