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Updated: Jun 28, 2026

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes
Published on: May 4, 2018
PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells
Lucia De Franceschi1, Andrea Biondani, Franco Carta
1Department of Clinical and Experimental Medicine, Section of Internal Medicine, University of Verona, Verona, Italy. lucia.defranceschi@univr.it
Abstract:
Protein tyrosine phosphatases (PTPs) are crucial components of cellular signal transduction pathways. Here, we report that red blood cells (RBCs) from mice lacking PTPepsilon (Ptpre(-/-)) exhibit (i) abnormal morphology; (ii) increased Ca(2+)-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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