Research ArticleBiochemistry

Tyrosine Kinase BMX Phosphorylates Phosphotyrosine-Primed Motif Mediating the Activation of Multiple Receptor Tyrosine Kinases

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Sci. Signal.  28 May 2013:
Vol. 6, Issue 277, pp. ra40
DOI: 10.1126/scisignal.2003936

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Primed for Activation

Various tyrosine kinases have dual tyrosine motifs in their kinase domains. Phosphorylation of the first is necessary for activity, but full activation requires phosphorylation of the second. Chen et al. showed that in vitro BMX (bone marrow tyrosine kinase gene on chromosome X) has a preference for these primed “pYY” motifs, only phosphorylating the second tyrosine if the first is already phosphorylated. Loss of BMX activity reduced FAK (focal adhesion kinase) activity and insulin receptor signaling, suggesting that BMX may enhance signaling by various tyrosine kinases that contain the pYY motif. These findings reveal a previously uncharacterized property of BMX that may be involved in the regulation of multiple tyrosine kinase pathways.