Dec 25, 2010

A tissue-specific atlas of mouse protein phosphorylation and expression

Cell
Edward L HuttlinSteven P Gygi

Abstract

Although most tissues in an organism are genetically identical, the biochemistry of each is optimized to fulfill its unique physiological roles, with important consequences for human health and disease. Each tissue's unique physiology requires tightly regulated gene and protein expression coordinated by specialized, phosphorylation-dependent intracellular signaling. To better understand the role of phosphorylation in maintenance of physiological differences among tissues, we performed proteomic and phosphoproteomic characterizations of nine mouse tissues. We identified 12,039 proteins, including 6296 phosphoproteins harboring nearly 36,000 phosphorylation sites. Comparing protein abundances and phosphorylation levels revealed specialized, interconnected phosphorylation networks within each tissue while suggesting that many proteins are regulated by phosphorylation independently of their expression. Our data suggest that the "typical" phosphoprotein is widely expressed yet displays variable, often tissue-specific phosphorylation that tunes protein activity to the specific needs of each tissue. We offer this dataset as an online resource for the biological research community.

  • References43
  • Citations611

Mentioned in this Paper

Pathologic Cytolysis
Vesicle-Associated Membrane Protein 1
Establishment and Maintenance of Localization
Brown Fat
Biochemical Pathway
Cyclic AMP-Responsive DNA-Binding Protein
Benign Neoplasm of Testis
Formicum acidum, formic acid, Homeopathic preparation
Acrylamide
Tissue Membrane

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