CPR scientists delineate protein phosphorylation sites across 14 different rat tissues and organs.
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
Protein phosphorylation is a post translational modification implicated in a diverse variety of cellular processes spanning from proliferation and differentiation to apoptosis. Site specific phosphorylation events often function as molecular switches that either activate or inhibit protein activity, and they have been implicated in the pathophysiology of several severe diseases, such as cancer, diabetes, and neuropsychiatric disorders. To better understand disease fingerprints and to evaluate which medical treatment is most appropriate for a patient, it would be beneficial if the phosphoproteome of tissue samples from patients could be analyzed. However, for such analyses to be feasible it is a prerequisite that reliable and comprehensive methods are developed. Scientists at CPR have used high resolution tandem mass spectrometry to generate the broadest tissue catalog of phosphorylated proteins to date, and the identified phosphorylation sites are localized to specific amino acids. The dataset generated covers 31,480 phosphorylation sites on 7,280 proteins quantified across 14 rat organs and tissues and is easily accessible to biologists via a web-based database. As the method developed by the CPR scientists is much simpler and faster than previously reported methods, it provides a promising platform for standardizing screening of tissue phosphoproteomes. The results have recently been published in Nature Communications.