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. 2015 Jan;37:66-72.
doi: 10.1016/j.semcdb.2014.09.021. Epub 2014 Sep 26.

Mining the Function of Protein Tyrosine Phosphatases in Health and Disease

Free PMC article

Mining the Function of Protein Tyrosine Phosphatases in Health and Disease

Hojin Lee et al. Semin Cell Dev Biol. .
Free PMC article


Protein tyrosine phosphatases (PTPs) play a crucial role in the regulation of human health and it is now clear that PTP dysfunction is causal to a variety of human diseases. Research in the PTP field has accelerated dramatically over the last decade fueled by cutting-edge technologies in genomic and proteomic techniques. This system-wide non-biased approach when applied to the discovery of PTP function has led to the elucidation of new and unanticipated roles for the PTPs. These discoveries, driven by genomic and proteomic approaches, have uncovered novel PTP findings that range from those that describe fundamental cell signaling mechanisms to implications for PTPs as novel therapeutic targets for the treatment of human disease. This review will discuss how new PTP functions have been uncovered through studies that have utilized genomic and proteomic technologies and strategies.

Keywords: Genomics; Phosphorylation; Protein tyrosine phosphatases; Proteomics; Signal transduction; Substrates.


Fig. 1
Fig. 1. Classical protein tyrosine phosphatase (PTP) family
Schematic of the classical non transmembrane and receptor-like protein tyrosine phosphatases.
Fig. 2
Fig. 2. The dual-specificity phosphatase (DUSP) family
Schematic of the dual specificity phosphatases, which are comprised of the sub-family of MAP kinase phosphatases (MKPs) and atypical DUSPs.
Fig. 3
Fig. 3. Schematic representation of approaches to identify PTP function and substrate
siRNA or shRNA can be selected according to the desired experimental situation. Substrates of PTPs can be identified using proteomic methods.
Fig. 4
Fig. 4. Schematic of phosphoproteomic analysis of differentially tyrosyl phosphorylated proteins in mouse models of disease
Proteomic approaches can be used to differentially determine relative levels of tyrosyl phosphorylated proteins which can be analyzed by enrichment with anti-phosphotyrosine antibodies. A combination of biochemical approaches can be applied in order to validate protein targets.

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