Abstract
Background: Syk is a tyrosine kinase with both tumor promoting and tumor suppressing activities in cancer cells. Results: Protein kinase A is phosphorylated on a C-terminal tyrosine by Syk. Conclusion: The phosphorylation of PKA inhibits its activity and its ability to activate CREB. Significance: The phosphorylation by Syk of PKA inhibits its participation in downstream signaling pathways. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Yu, S., Huang, H., Iliuk, A., Wang, W. H., Jayasundera, K. B., Tao, W. A., … Geahlen, R. L. (2013). Syk inhibits the activity of protein kinase a by phosphorylating tyrosine 330 of the catalytic subunit. Journal of Biological Chemistry, 288(15), 10870–10881. https://doi.org/10.1074/jbc.M112.426130
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