J. William Tanner

TL;DR: The results suggest that the interactions of 14-3-3 with signaling proteins are critical for the activation of signaling proteins and suggest novel roles for serine/threonine phosphorylation in the assembly of protein-protein complexes.

TL;DR: It is demonstrated that chimeric cytokine receptors which contain the cytoplasmic domain of the receptors for GH and EPO or for gp130 can form complexes with JAK2 when transiently co-expressed in HeLa cells.

TL;DR: A requirement for 14-3-3 for Raf-1 kinase activity and phosphorylation is demonstrated, which supports a paradigm in which the effects of phosphorylated proteins on serine as well as tyrosine residues are mediated by inducible protein-protein interactions.

TL;DR: A site in the IFN- receptor α chain required for constitutive JAK-1 association is identified and it is established that this association is critical forIFN- signal transduction.

TL;DR: The retrovirally transduced the erythropoietin receptor or a constitutively activated form of the EPOR into normal hematopoietic progenitors, including blast cell colonies, and determined that the EPO-R box 1 cytoplasmic motif is required for the binding and activation of JAK2.