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PTPε has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells

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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DOI: 10.1002/pmic.200700596


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.

Item Type:Article
ID Code:1869
Uncontrolled Keywords:Fyn, Gardos channel, Syk, Tyrosine-phosphorylation
Subjects:Area 05 - Scienze biologiche > BIO/10 Biochimica
Area 06 - Scienze mediche > MED/04 Patologia generale
Divisions:002 Altri enti e centri di ricerca del Nord Sardegna > Nurex Bioresearch Sassari, Sassari
Deposited On:18 Aug 2009 10:06

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