Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling

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Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling. / Eguchi, Akihiro; Olsen, Jesper V.

In: Scientific Reports, Vol. 14, 7908, 2024.

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

Harvard

Eguchi, A & Olsen, JV 2024, 'Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling', Scientific Reports, vol. 14, 7908. https://doi.org/10.1038/s41598-024-58619-1

APA

Eguchi, A., & Olsen, J. V. (2024). Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling. Scientific Reports, 14, [7908]. https://doi.org/10.1038/s41598-024-58619-1

Vancouver

Eguchi A, Olsen JV. Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling. Scientific Reports. 2024;14. 7908. https://doi.org/10.1038/s41598-024-58619-1

Author

Eguchi, Akihiro ; Olsen, Jesper V. / Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling. In: Scientific Reports. 2024 ; Vol. 14.

Bibtex

@article{c72471e76e2647c8923be3c2d2a7c6a5,
title = "Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling",
abstract = "Receptor tyrosine kinases (RTKs) initiate cellular signaling pathways, which are regulated through a delicate balance of phosphorylation and dephosphorylation events. While many studies of RTKs have focused on downstream-activated kinases catalyzing the site-specific phosphorylation, few studies have focused on the phosphatases carrying out the dephosphorylation. In this study, we analyzed six protein phosphatase networks using chemical inhibitors in context of epidermal growth factor receptor (EGFR) signaling by mass spectrometry-based phosphoproteomics. Specifically, we focused on protein phosphatase 2C (PP2C), involved in attenuating p38-dependent signaling pathways in various cellular responses, and confirmed its effect in regulating p38 activity in EGFR signaling. Furthermore, utilizing a p38 inhibitor, we classified phosphosites whose phosphorylation status depends on PP2C inhibition into p38-dependent and p38-independent sites. This study provides a large-scale dataset of phosphatase-regulation of EGF-responsive phosphorylation sites, which serves as a useful resource to deepen our understanding of EGFR signaling.",
keywords = "ErbB Receptors/metabolism, Signal Transduction, Phosphorylation, Phosphoprotein Phosphatases/metabolism",
author = "Akihiro Eguchi and Olsen, {Jesper V}",
note = "{\textcopyright} 2024. The Author(s).",
year = "2024",
doi = "10.1038/s41598-024-58619-1",
language = "English",
volume = "14",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling

AU - Eguchi, Akihiro

AU - Olsen, Jesper V

N1 - © 2024. The Author(s).

PY - 2024

Y1 - 2024

N2 - Receptor tyrosine kinases (RTKs) initiate cellular signaling pathways, which are regulated through a delicate balance of phosphorylation and dephosphorylation events. While many studies of RTKs have focused on downstream-activated kinases catalyzing the site-specific phosphorylation, few studies have focused on the phosphatases carrying out the dephosphorylation. In this study, we analyzed six protein phosphatase networks using chemical inhibitors in context of epidermal growth factor receptor (EGFR) signaling by mass spectrometry-based phosphoproteomics. Specifically, we focused on protein phosphatase 2C (PP2C), involved in attenuating p38-dependent signaling pathways in various cellular responses, and confirmed its effect in regulating p38 activity in EGFR signaling. Furthermore, utilizing a p38 inhibitor, we classified phosphosites whose phosphorylation status depends on PP2C inhibition into p38-dependent and p38-independent sites. This study provides a large-scale dataset of phosphatase-regulation of EGF-responsive phosphorylation sites, which serves as a useful resource to deepen our understanding of EGFR signaling.

AB - Receptor tyrosine kinases (RTKs) initiate cellular signaling pathways, which are regulated through a delicate balance of phosphorylation and dephosphorylation events. While many studies of RTKs have focused on downstream-activated kinases catalyzing the site-specific phosphorylation, few studies have focused on the phosphatases carrying out the dephosphorylation. In this study, we analyzed six protein phosphatase networks using chemical inhibitors in context of epidermal growth factor receptor (EGFR) signaling by mass spectrometry-based phosphoproteomics. Specifically, we focused on protein phosphatase 2C (PP2C), involved in attenuating p38-dependent signaling pathways in various cellular responses, and confirmed its effect in regulating p38 activity in EGFR signaling. Furthermore, utilizing a p38 inhibitor, we classified phosphosites whose phosphorylation status depends on PP2C inhibition into p38-dependent and p38-independent sites. This study provides a large-scale dataset of phosphatase-regulation of EGF-responsive phosphorylation sites, which serves as a useful resource to deepen our understanding of EGFR signaling.

KW - ErbB Receptors/metabolism

KW - Signal Transduction

KW - Phosphorylation

KW - Phosphoprotein Phosphatases/metabolism

U2 - 10.1038/s41598-024-58619-1

DO - 10.1038/s41598-024-58619-1

M3 - Journal article

C2 - 38575675

VL - 14

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 7908

ER -

ID: 389359741