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

TY - JOUR

T1 - Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues

AU - Lundby, Alicia

AU - Secher, Anna

AU - Lage, Kasper

AU - Nordsborg, Nikolai B

AU - Dmytriyev, Anatoliy

AU - Lundby, Carsten

AU - Olsen, Jesper V

N1 - CURIS 2012 5200 068

PY - 2012/6/6

Y1 - 2012/6/6

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms1871

DO - 10.1038/ncomms1871

M3 - Journal article

C2 - 22673903

SN - 2041-1723

VL - 3

SP - 1

EP - 10

JO - Nature Communications

JF - Nature Communications

M1 - Article 876

ER -