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Cell signalling

It's good to talk

Nature Reviews Molecular Cell Biology volume 11, pages 88–89 (2010)Cite this article

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To study bidirectional EphR–ephrin signalling in the context of direct cell–cell interactions, the authors labelled cells expressing EphB2 or ephrin B1 using different amino acid isotopes, which enable relative quantification of Tyr phosphorylation peptides (and therefore signalling events) by mass spectrometry in a cell line-specific manner. They found that global changes in Tyr phosphorylation induced by cell–cell contact differ between the two cell types. The comparison of cell-specific modulation of the 100 Tyr phosphorylation sites present in both cell types identified asymmetric regulation of proteins that have a wide range of molecular and cellular functions. For example, the phosphorylation of adaptor proteins is preferentially increased in EphB2-expressing cells, suggesting that they have cell-specific regulatory roles.

“the asymmetric regulation of Tyr phosphorylation events in EphB2- and ephrin B1-expressing cells is achieved through the alternative use of kinases and adaptor proteins.”

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ORIGINAL RESEARCH PAPER

  1. Jørgensen, C. et al. Cell-specific information processing in segregating populations of Eph receptor ephrin–expressing cells. Science 326, 1502–1509 (2009)

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  1. Francesca Cesari
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Cesari, F. It's good to talk. Nat Rev Mol Cell Biol 11, 88–89 (2010). https://doi.org/10.1038/nrm2837

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