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Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues

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  • Alicia Lundby

    (Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
    The Danish National Research Foundation Centre for Cardiac Arrhythmia, University of Copenhagen, 2100)

  • Anna Secher

    (Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
    Novo Nordisk A/S, Novo Nordisk Park)

  • Kasper Lage

    (Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
    Pediatric Surgical Research Laboratory, Massachusets General Hospital
    Harvard Medical School
    The Broad Institute of MIT and Harvard)

  • Nikolai B. Nordsborg

    (University of Copenhagen, Universitetsparken 13)

  • Anatoliy Dmytriyev

    (Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.)

  • Carsten Lundby

    (Zürich Centre for Integrative Human Physiology, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.)

  • Jesper V. Olsen

    (Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.)

Abstract

Deregulated cellular signalling is a common hallmark of disease, and delineating tissue phosphoproteomes is key to unravelling the underlying mechanisms. Here we present the broadest tissue catalogue of phosphoproteins to date, covering 31,480 phosphorylation sites on 7,280 proteins quantified across 14 rat organs and tissues. We provide the data set as an easily accessible resource via a web-based database, the CPR PTM Resource. A major fraction of the presented phosphorylation sites are tissue-specific and modulate protein interaction networks that are essential for the function of individual organs. For skeletal muscle, we find that phosphotyrosines are over-represented, which is mainly due to proteins involved in glycogenolysis and muscle contraction, a finding we validate in human skeletal muscle biopsies. Tyrosine phosphorylation is involved in both skeletal and cardiac muscle contraction, whereas glycogenolytic enzymes are tyrosine phosphorylated in skeletal muscle but not in the liver. The presented phosphoproteomic method is simple and rapid, making it applicable for screening of diseased tissue samples.

Suggested Citation

  • Alicia Lundby & Anna Secher & Kasper Lage & Nikolai B. Nordsborg & Anatoliy Dmytriyev & Carsten Lundby & Jesper V. Olsen, 2012. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues," Nature Communications, Nature, vol. 3(1), pages 1-10, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1871
    DOI: 10.1038/ncomms1871
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    Cited by:

    1. Yafei Yuan & Fang Kong & Hanwen Xu & Angqi Zhu & Nieng Yan & Chuangye Yan, 2022. "Cryo-EM structure of human glucose transporter GLUT4," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    2. Tiziano Mazza & Theodoros I. Roumeliotis & Elena Garitta & David Drew & S. Tamir Rashid & Cesare Indiveri & Jyoti S. Choudhary & Kenneth J. Linton & Konstantinos Beis, 2024. "Structural basis for the modulation of MRP2 activity by phosphorylation and drugs," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Yu Zong & Yuxin Wang & Yi Yang & Dan Zhao & Xiaoqing Wang & Chengpin Shen & Liang Qiao, 2023. "DeepFLR facilitates false localization rate control in phosphoproteomics," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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