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Quantitative interaction proteomics of neurodegenerative disease proteins

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Quantitative interaction proteomics of neurodegenerative disease proteins. / Hosp, Fabian; Vossfeldt, Hannes; Heinig, Matthias; Vasiljevic, Djordje; Arumughan, Anup; Wyler, Emanuel; Landthaler, Markus; Hubner, Norbert; Wanker, Erich E; Lannfelt, Lars; Ingelsson, Martin; Lalowski, Maciej; Voigt, Aaron; Selbach, Matthias; Genetic and Environmental Risk for Alzheimer’s disease (GERAD1) Consortium.

In: CELL REP, Vol. 11, No. 7, 19.05.2015, p. 1134-46.

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

Harvard

Hosp, F, Vossfeldt, H, Heinig, M, Vasiljevic, D, Arumughan, A, Wyler, E, Landthaler, M, Hubner, N, Wanker, EE, Lannfelt, L, Ingelsson, M, Lalowski, M, Voigt, A, Selbach, M & Genetic and Environmental Risk for Alzheimer’s disease (GERAD1) Consortium 2015, 'Quantitative interaction proteomics of neurodegenerative disease proteins', CELL REP, vol. 11, no. 7, pp. 1134-46. https://doi.org/10.1016/j.celrep.2015.04.030

APA

Hosp, F., Vossfeldt, H., Heinig, M., Vasiljevic, D., Arumughan, A., Wyler, E., Landthaler, M., Hubner, N., Wanker, E. E., Lannfelt, L., Ingelsson, M., Lalowski, M., Voigt, A., Selbach, M., & Genetic and Environmental Risk for Alzheimer’s disease (GERAD1) Consortium (2015). Quantitative interaction proteomics of neurodegenerative disease proteins. CELL REP, 11(7), 1134-46. https://doi.org/10.1016/j.celrep.2015.04.030

Vancouver

Hosp F, Vossfeldt H, Heinig M, Vasiljevic D, Arumughan A, Wyler E et al. Quantitative interaction proteomics of neurodegenerative disease proteins. CELL REP. 2015 May 19;11(7):1134-46. https://doi.org/10.1016/j.celrep.2015.04.030

Bibtex

@article{531f840413424343b08e0ffc2e1e7cd2,
title = "Quantitative interaction proteomics of neurodegenerative disease proteins",
abstract = "Several proteins have been linked to neurodegenerative disorders (NDDs), but their molecular function is not completely understood. Here, we used quantitative interaction proteomics to identify binding partners of Amyloid beta precursor protein (APP) and Presenilin-1 (PSEN1) for Alzheimer's disease (AD), Huntingtin (HTT) for Huntington's disease, Parkin (PARK2) for Parkinson's disease, and Ataxin-1 (ATXN1) for spinocerebellar ataxia type 1. Our network reveals common signatures of protein degradation and misfolding and recapitulates known biology. Toxicity modifier screens and comparison to genome-wide association studies show that interaction partners are significantly linked to disease phenotypes in vivo. Direct comparison of wild-type proteins and disease-associated variants identified binders involved in pathogenesis, highlighting the value of differential interactome mapping. Finally, we show that the mitochondrial protein LRPPRC interacts preferentially with an early-onset AD variant of APP. This interaction appears to induce mitochondrial dysfunction, which is an early phenotype of AD.",
author = "Fabian Hosp and Hannes Vossfeldt and Matthias Heinig and Djordje Vasiljevic and Anup Arumughan and Emanuel Wyler and Markus Landthaler and Norbert Hubner and Wanker, {Erich E} and Lars Lannfelt and Martin Ingelsson and Maciej Lalowski and Aaron Voigt and Matthias Selbach and {Genetic and Environmental Risk for Alzheimer{\textquoteright}s disease (GERAD1) Consortium}",
note = "Copyright {\textcopyright} 2015 The Authors. Published by Elsevier Inc. All rights reserved.",
year = "2015",
month = may,
day = "19",
doi = "10.1016/j.celrep.2015.04.030",
language = "English",
volume = "11",
pages = "1134--46",
journal = "CELL REP",
issn = "2211-1247",
publisher = "Elsevier",
number = "7",

}

RIS

TY - JOUR

T1 - Quantitative interaction proteomics of neurodegenerative disease proteins

AU - Hosp, Fabian

AU - Vossfeldt, Hannes

AU - Heinig, Matthias

AU - Vasiljevic, Djordje

AU - Arumughan, Anup

AU - Wyler, Emanuel

AU - Landthaler, Markus

AU - Hubner, Norbert

AU - Wanker, Erich E

AU - Lannfelt, Lars

AU - Ingelsson, Martin

AU - Lalowski, Maciej

AU - Voigt, Aaron

AU - Selbach, Matthias

AU - Genetic and Environmental Risk for Alzheimer’s disease (GERAD1) Consortium

N1 - Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2015/5/19

Y1 - 2015/5/19

N2 - Several proteins have been linked to neurodegenerative disorders (NDDs), but their molecular function is not completely understood. Here, we used quantitative interaction proteomics to identify binding partners of Amyloid beta precursor protein (APP) and Presenilin-1 (PSEN1) for Alzheimer's disease (AD), Huntingtin (HTT) for Huntington's disease, Parkin (PARK2) for Parkinson's disease, and Ataxin-1 (ATXN1) for spinocerebellar ataxia type 1. Our network reveals common signatures of protein degradation and misfolding and recapitulates known biology. Toxicity modifier screens and comparison to genome-wide association studies show that interaction partners are significantly linked to disease phenotypes in vivo. Direct comparison of wild-type proteins and disease-associated variants identified binders involved in pathogenesis, highlighting the value of differential interactome mapping. Finally, we show that the mitochondrial protein LRPPRC interacts preferentially with an early-onset AD variant of APP. This interaction appears to induce mitochondrial dysfunction, which is an early phenotype of AD.

AB - Several proteins have been linked to neurodegenerative disorders (NDDs), but their molecular function is not completely understood. Here, we used quantitative interaction proteomics to identify binding partners of Amyloid beta precursor protein (APP) and Presenilin-1 (PSEN1) for Alzheimer's disease (AD), Huntingtin (HTT) for Huntington's disease, Parkin (PARK2) for Parkinson's disease, and Ataxin-1 (ATXN1) for spinocerebellar ataxia type 1. Our network reveals common signatures of protein degradation and misfolding and recapitulates known biology. Toxicity modifier screens and comparison to genome-wide association studies show that interaction partners are significantly linked to disease phenotypes in vivo. Direct comparison of wild-type proteins and disease-associated variants identified binders involved in pathogenesis, highlighting the value of differential interactome mapping. Finally, we show that the mitochondrial protein LRPPRC interacts preferentially with an early-onset AD variant of APP. This interaction appears to induce mitochondrial dysfunction, which is an early phenotype of AD.

U2 - 10.1016/j.celrep.2015.04.030

DO - 10.1016/j.celrep.2015.04.030

M3 - SCORING: Journal article

C2 - 25959826

VL - 11

SP - 1134

EP - 1146

JO - CELL REP

JF - CELL REP

SN - 2211-1247

IS - 7

ER -