PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.
作者： Lucia De Franceschi , Andrea Biondani , Franco Carta , Franco Turrini , Carlo Laudanna
关键词:
摘要: Protein tyrosine phosphatases (PTPs) are crucial components of cellular signal transduction pathways. We report here that red blood cells (RBCs) from mice lacking PTPe (Ptpre −/− ) exhibit abnormal morphology and increased Ca 2+ -activated-K + channel activity, which was partially blocked by the Src-Family-Kinases (SFKs) inhibitor PP1. In Ptpre mouse RBCs, activity Fyn Yes, two SFKs, were increased, suggesting a functional relationship between -channel. The absence markedly affected RBC membrane (Tyr-) phosphoproteome, indicating perturbation RBCs Using signaling network computational analysis Tyr-phosphoproteomic data, we identified 7 topological clusters. studied cluster 1, containing Syk-Tyr-kinase: Syk-kinase higher in wild-type than validating novel pathway, involves Syk regulation cell morphology.
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