The role of serine/threonine phosphorylation in hematopoietic cytokine receptor signal transduction

The hematopoietic cytokine receptors rapidly activate tyrosine phosphorylation after ligand engagement. In addition, however, serine/ threonine phosphorylation of important effector molecules also icreases. Interleukins 2‐5 and gran‐ulocyte‐macrophage colony stimulating factor all activate protein kinase C. This results in serine/threonine phosphorylation of such important regulatory molecules as Raf‐1 kinase, myristoylated alanine‐ rich C kinase substrate, and SOS. These phos‐ phorylated effector molecules are regulators of important genes related to cell survival and proliferation. In addition, as yet uncharacterized serine/ threonine kinases associate directly with the hematopoietic receptor subunits themselves. These kinases may contribute to the phosphorylation of the STAT family of transcription factors that is important in regulating cytokine‐specific gene inductions. Thus, it is time to begin integrating serine/threonine kinases into the postulated signaling pathways activated by hematopoietic cytokine receptors.— Mufson, R. A. The role of serine/threonine phosphorylation in hematopoietic cytokine receptor signal transduction. FASEB J. 11, 37‐44 (1997)

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