Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics

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Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics. / Flury, Valentin; Restuccia, Umberto; Bachi, Angela; Mühlemann, Oliver.

In: Journal of Proteome Research, Vol. 13, No. 6, 2014, p. 3038-3053.

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

Harvard

Flury, V, Restuccia, U, Bachi, A & Mühlemann, O 2014, 'Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics', Journal of Proteome Research, vol. 13, no. 6, pp. 3038-3053. https://doi.org/10.1021/pr5002143

APA

Flury, V., Restuccia, U., Bachi, A., & Mühlemann, O. (2014). Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics. Journal of Proteome Research, 13(6), 3038-3053. https://doi.org/10.1021/pr5002143

Vancouver

Flury V, Restuccia U, Bachi A, Mühlemann O. Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics. Journal of Proteome Research. 2014;13(6):3038-3053. https://doi.org/10.1021/pr5002143

Author

Flury, Valentin ; Restuccia, Umberto ; Bachi, Angela ; Mühlemann, Oliver. / Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics. In: Journal of Proteome Research. 2014 ; Vol. 13, No. 6. pp. 3038-3053.

Bibtex

@article{fbeb6a9547ad4f3984df97f2901faecd,
title = "Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics",
abstract = "Human up-frameshift 1 (UPF1) is an ATP-dependent RNA helicase and phosphoprotein implicated in several biological processes but is best known for its key function in nonsense-mediated mRNA decay (NMD). Here we employed a combination of stable isotope labeling of amino acids in cell culture experiments to determine by quantitative proteomics UPF1 interactors. We used this approach to distinguish between RNA-mediated and protein-mediated UPF1 interactors and to determine proteins that preferentially bind the hypo- or the hyper-phosphorylated form of UPF1. Confirming and expanding previous studies, we identified the eukaryotic initiation factor 3 (eIF3) as a prominent protein-mediated interactor of UPF1. However, unlike previously reported, eIF3 binds to UPF1 independently of UPF1's phosphorylation state. Furthermore, our data revealed many nucleus-associated RNA-binding proteins that preferentially associate with hyper-phosphorylated UPF1 in an RNase-sensitive manner, suggesting that UPF1 gets recruited to mRNA and becomes phosphorylated before being exported to the cytoplasm as part of the mRNP.",
keywords = "eIF3, NMD, RENT1, SILAC, STRAP, THO complex, TREX, UNRIP, UPF1",
author = "Valentin Flury and Umberto Restuccia and Angela Bachi and Oliver M{\"u}hlemann",
year = "2014",
doi = "10.1021/pr5002143",
language = "English",
volume = "13",
pages = "3038--3053",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "6",

}

RIS

TY - JOUR

T1 - Characterization of phosphorylation- and RNA-dependent UPF1 interactors by quantitative proteomics

AU - Flury, Valentin

AU - Restuccia, Umberto

AU - Bachi, Angela

AU - Mühlemann, Oliver

PY - 2014

Y1 - 2014

N2 - Human up-frameshift 1 (UPF1) is an ATP-dependent RNA helicase and phosphoprotein implicated in several biological processes but is best known for its key function in nonsense-mediated mRNA decay (NMD). Here we employed a combination of stable isotope labeling of amino acids in cell culture experiments to determine by quantitative proteomics UPF1 interactors. We used this approach to distinguish between RNA-mediated and protein-mediated UPF1 interactors and to determine proteins that preferentially bind the hypo- or the hyper-phosphorylated form of UPF1. Confirming and expanding previous studies, we identified the eukaryotic initiation factor 3 (eIF3) as a prominent protein-mediated interactor of UPF1. However, unlike previously reported, eIF3 binds to UPF1 independently of UPF1's phosphorylation state. Furthermore, our data revealed many nucleus-associated RNA-binding proteins that preferentially associate with hyper-phosphorylated UPF1 in an RNase-sensitive manner, suggesting that UPF1 gets recruited to mRNA and becomes phosphorylated before being exported to the cytoplasm as part of the mRNP.

AB - Human up-frameshift 1 (UPF1) is an ATP-dependent RNA helicase and phosphoprotein implicated in several biological processes but is best known for its key function in nonsense-mediated mRNA decay (NMD). Here we employed a combination of stable isotope labeling of amino acids in cell culture experiments to determine by quantitative proteomics UPF1 interactors. We used this approach to distinguish between RNA-mediated and protein-mediated UPF1 interactors and to determine proteins that preferentially bind the hypo- or the hyper-phosphorylated form of UPF1. Confirming and expanding previous studies, we identified the eukaryotic initiation factor 3 (eIF3) as a prominent protein-mediated interactor of UPF1. However, unlike previously reported, eIF3 binds to UPF1 independently of UPF1's phosphorylation state. Furthermore, our data revealed many nucleus-associated RNA-binding proteins that preferentially associate with hyper-phosphorylated UPF1 in an RNase-sensitive manner, suggesting that UPF1 gets recruited to mRNA and becomes phosphorylated before being exported to the cytoplasm as part of the mRNP.

KW - eIF3

KW - NMD

KW - RENT1

KW - SILAC

KW - STRAP

KW - THO complex

KW - TREX

KW - UNRIP

KW - UPF1

U2 - 10.1021/pr5002143

DO - 10.1021/pr5002143

M3 - Journal article

C2 - 24762188

AN - SCOPUS:84902094509

VL - 13

SP - 3038

EP - 3053

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 6

ER -

ID: 337388350