Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

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

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Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. / Woerner, Andreas C; Frottin, Frédéric; Hornburg, Daniel; Feng, Li R; Meissner, Felix; Patra, Maria; Tatzelt, Jörg; Mann, Matthias; Winklhofer, Konstanze F; Hartl, F Ulrich; Hipp, Mark S.

In: Science (New York, N.Y.), Vol. 351, No. 6269, 08.01.2016, p. 173-6.

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

Harvard

Woerner, AC, Frottin, F, Hornburg, D, Feng, LR, Meissner, F, Patra, M, Tatzelt, J, Mann, M, Winklhofer, KF, Hartl, FU & Hipp, MS 2016, 'Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA', Science (New York, N.Y.), vol. 351, no. 6269, pp. 173-6. https://doi.org/10.1126/science.aad2033

APA

Woerner, A. C., Frottin, F., Hornburg, D., Feng, L. R., Meissner, F., Patra, M., Tatzelt, J., Mann, M., Winklhofer, K. F., Hartl, F. U., & Hipp, M. S. (2016). Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. Science (New York, N.Y.), 351(6269), 173-6. https://doi.org/10.1126/science.aad2033

Vancouver

Woerner AC, Frottin F, Hornburg D, Feng LR, Meissner F, Patra M et al. Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. Science (New York, N.Y.). 2016 Jan 8;351(6269):173-6. https://doi.org/10.1126/science.aad2033

Author

Woerner, Andreas C ; Frottin, Frédéric ; Hornburg, Daniel ; Feng, Li R ; Meissner, Felix ; Patra, Maria ; Tatzelt, Jörg ; Mann, Matthias ; Winklhofer, Konstanze F ; Hartl, F Ulrich ; Hipp, Mark S. / Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. In: Science (New York, N.Y.). 2016 ; Vol. 351, No. 6269. pp. 173-6.

Bibtex

@article{4c244b3bdeb0420d804f379d3c265ddf,
title = "Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA",
abstract = "Amyloid-like protein aggregation is associated with neurodegeneration and other pathologies. The nature of the toxic aggregate species and their mechanism of action remain elusive. Here, we analyzed the compartment specificity of aggregate toxicity using artificial β-sheet proteins, as well as fragments of mutant huntingtin and TAR DNA binding protein-43 (TDP-43). Aggregation in the cytoplasm interfered with nucleocytoplasmic protein and RNA transport. In contrast, the same proteins did not inhibit transport when forming inclusions in the nucleus at or around the nucleolus. Protein aggregation in the cytoplasm, but not the nucleus, caused the sequestration and mislocalization of proteins containing disordered and low-complexity sequences, including multiple factors of the nuclear import and export machinery. Thus, impairment of nucleocytoplasmic transport may contribute to the cellular pathology of various aggregate deposition diseases.",
keywords = "Active Transport, Cell Nucleus, Cell Nucleus, Cytoplasm, DNA-Binding Proteins, HEK293 Cells, Humans, Huntingtin Protein, Nerve Tissue Proteins, Neurodegenerative Diseases, Protein Aggregates, Protein Structure, Secondary, RNA, Messenger, Journal Article, Research Support, Non-U.S. Gov't",
author = "Woerner, {Andreas C} and Fr{\'e}d{\'e}ric Frottin and Daniel Hornburg and Feng, {Li R} and Felix Meissner and Maria Patra and J{\"o}rg Tatzelt and Matthias Mann and Winklhofer, {Konstanze F} and Hartl, {F Ulrich} and Hipp, {Mark S}",
note = "Copyright {\textcopyright} 2016, American Association for the Advancement of Science.",
year = "2016",
month = jan,
day = "8",
doi = "10.1126/science.aad2033",
language = "English",
volume = "351",
pages = "173--6",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6269",

}

RIS

TY - JOUR

T1 - Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

AU - Woerner, Andreas C

AU - Frottin, Frédéric

AU - Hornburg, Daniel

AU - Feng, Li R

AU - Meissner, Felix

AU - Patra, Maria

AU - Tatzelt, Jörg

AU - Mann, Matthias

AU - Winklhofer, Konstanze F

AU - Hartl, F Ulrich

AU - Hipp, Mark S

N1 - Copyright © 2016, American Association for the Advancement of Science.

PY - 2016/1/8

Y1 - 2016/1/8

N2 - Amyloid-like protein aggregation is associated with neurodegeneration and other pathologies. The nature of the toxic aggregate species and their mechanism of action remain elusive. Here, we analyzed the compartment specificity of aggregate toxicity using artificial β-sheet proteins, as well as fragments of mutant huntingtin and TAR DNA binding protein-43 (TDP-43). Aggregation in the cytoplasm interfered with nucleocytoplasmic protein and RNA transport. In contrast, the same proteins did not inhibit transport when forming inclusions in the nucleus at or around the nucleolus. Protein aggregation in the cytoplasm, but not the nucleus, caused the sequestration and mislocalization of proteins containing disordered and low-complexity sequences, including multiple factors of the nuclear import and export machinery. Thus, impairment of nucleocytoplasmic transport may contribute to the cellular pathology of various aggregate deposition diseases.

AB - Amyloid-like protein aggregation is associated with neurodegeneration and other pathologies. The nature of the toxic aggregate species and their mechanism of action remain elusive. Here, we analyzed the compartment specificity of aggregate toxicity using artificial β-sheet proteins, as well as fragments of mutant huntingtin and TAR DNA binding protein-43 (TDP-43). Aggregation in the cytoplasm interfered with nucleocytoplasmic protein and RNA transport. In contrast, the same proteins did not inhibit transport when forming inclusions in the nucleus at or around the nucleolus. Protein aggregation in the cytoplasm, but not the nucleus, caused the sequestration and mislocalization of proteins containing disordered and low-complexity sequences, including multiple factors of the nuclear import and export machinery. Thus, impairment of nucleocytoplasmic transport may contribute to the cellular pathology of various aggregate deposition diseases.

KW - Active Transport, Cell Nucleus

KW - Cell Nucleus

KW - Cytoplasm

KW - DNA-Binding Proteins

KW - HEK293 Cells

KW - Humans

KW - Huntingtin Protein

KW - Nerve Tissue Proteins

KW - Neurodegenerative Diseases

KW - Protein Aggregates

KW - Protein Structure, Secondary

KW - RNA, Messenger

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1126/science.aad2033

DO - 10.1126/science.aad2033

M3 - Journal article

C2 - 26634439

VL - 351

SP - 173

EP - 176

JO - Science

JF - Science

SN - 0036-8075

IS - 6269

ER -

ID: 186877743