= B. A. Witthuhn
{c}
<B. A. Witthuhn> is the first author of a 1993 study connecting the <erythropoietin receptor> to the <protein kinase> <JAK2>. The biological puzzle was how <erythropoietin> could stimulate <tyrosine phosphorylation> through a <receptor> that lacks its own kinase <protein domain>. The experiments showed that <JAK2> physically associates with an intracellular region of the <erythropoietin receptor>.<JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin by B. A. Witthuhn and others>[Abstract; Cell 74, 227–236, 1993]{ref}
Adding <erythropoietin> induced <JAK2> <tyrosine phosphorylation> and increased its <autophosphorylation> activity. Experiments with altered <erythropoietin receptors> connected these changes with the ability to stimulate cell multiplication. This supplied a concrete mechanism for <signal transduction>: a <receptor> without an intrinsic kinase <protein domain> can recruit a separate <protein kinase>. The combination of physical association, regulated activity and altered-receptor tests is more informative than any one measurement alone.<JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin by B. A. Witthuhn and others>[Abstract: receptor mutants, JAK2 association and activation correlated with mitogenesis]{ref}
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