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

Alicia Lundby, Anna Secher, Kasper Lage, Nikolai B. Nordsborg, Anatoliy Dmytriyev, Carsten Lundby and Jesper V. Olsen ()
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Alicia Lundby: Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
Anna Secher: Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
Kasper Lage: Faculty of Health Sciences, NNF Center for Protein Research, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen, Denmark.
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.

Nature Communications, 2012, vol. 3, issue 1, 1-10

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms1871

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