De Franceschi, Lucia and Biondani, Andrea and Carta, Franco and Turrini, Francesco Michelangelo and Laudanna, Carlo and Deana, Renzo and Brunati, Anna Maria and Turretta, Loris and Iolascon, Achille and Perrotta, Silverio and Elson, Ari and Bulato, Cristina and Brugnara, Carlo (2008) PTPε has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells. Proteomics, Vol. 8 (22), p. 4695-4708. eISSN 1615-9861. Article.
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Protein tyrosine phosphatases (PTPs) are crucial components of cellular signal transduction pathways. Here, we report that red blood cells (RBCs) from mice lacking PTP (Ptprε-/-) exhibit (i) abnormal morphology; (ii) increased Ca2+-activated-K+ channel activity, which was partially blocked by the Src family kinases (SFKs) inhibitor PP1; and (iii) market perturbation of the RBC membrane tyrosine (Tyr-) phosphoproteome, indicating an alteration of RBC signal transduction pathways. Using the signaling network computational analysis of the Tyr-phosphoproteomic data, we identified seven topological clusters. We studied cluster 1 containing Fyn, SFK, and Syk another tyrosine kinase. In Ptpre-/- mouse RBCs, the activity of Fyn was increased while Syk kinase activity was decreased compared to wild-type RBCs, validating the network computational analysis, and indicating a novel signaling pathway, which involves Fyn and Syk in regulation of red cell morphology.
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