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. 1993 Sep 15;90(18):8429–8433. doi: 10.1073/pnas.90.18.8429

Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction.

O Silvennoinen 1, B A Witthuhn 1, F W Quelle 1, J L Cleveland 1, T Yi 1, J N Ihle 1
PMCID: PMC47370  PMID: 8378315

Abstract

Interleukin 3 (IL-3) regulates the proliferation and differentiation of hematopoietic cells. Although the IL-3 receptor chains lack kinase catalytic domains, IL-3 induces tyrosine phosphorylation of cellular proteins. To investigate the potential role of the JAK family of protein-tyrosine kinases in IL-3 signal transduction, we have obtained full-length cDNA clones for murine Jak1 and Jak2 protein-tyrosine kinases and prepared antiserum against the predicted proteins. Using antisera against Jak2, we demonstrate that IL-3 stimulation results in the rapid and specific tyrosine phosphorylation of Jak2 and activates its in vitro kinase activity.

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