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Editorial
. 2013 Sep 1;12(17):2707-8.
doi: 10.4161/cc.25883. Epub 2013 Aug 6.

Phosphoproteomics taken to heart

Alicia Lundby  1 , Jesper V Olsen
Affiliations
Editorial

Phosphoproteomics taken to heart

Alicia Lundby et al. Cell Cycle. .
No abstract available

Keywords: KCNQ1; Kv7.1; beta-adrenergic signaling; beta-blocker; cardiac kinase regulation; cardiac signaling; cell signaling pathways; in vivo phosphoproteomics; ion channel phosphorylation; quantitative phosphoproteomics.

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Figures

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Figure 1. Experimental procedure: 2 groups of mice were treated with either blockers against β1AR and β2AR (control animals) or with a blocker against β2AR and an activator of β1AR (β1AR animals). β1AR animals were stimulated for 10 min. Proteins were extracted from the cardiac tissue and digested with trypsin followed by phosphopeptide enrichment by titanium-dioxide chromatography. The resulting samples were analyzed by high-resolution orbitrap tandem mass spectrometry to a depth of more than 4000 phosphorylated proteins containing more than 8500 phosphorylation sites. We quantified the phosphoproteins and phosphorylation sites between the 2 groups of mice. Six hundred and seventy phosphorylation sites were statistically significantly regulated in the β1AR animals compared with the control animals. The results highlighted several unexpected protein kinases with a sequence-specific preference of R-X-X-pS/T, as well as pinpointing the exact amino acid regulated by phosphorylation on key proteins involved in cardiac excitation–contraction coupling (figure adapted from Lundby et al.).
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References

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    1. Lundby A, et al. Cell Rep. 2012;2:419–31. doi: 10.1016/j.celrep.2012.07.006. - DOI - PMC - PubMed
    1. Lundby A, et al. Nat Commun. 2012;3:876. doi: 10.1038/ncomms1871. - DOI - PMC - PubMed

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