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

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.

SUBMITTER: Silvennoinen O

PROVIDER: S-EPMC47370 | biostudies-other | 1993 Sep

REPOSITORIES: biostudies-other

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

Silvennoinen O O Witthuhn B A BA Quelle F W FW Cleveland J L JL Yi T T Ihle J N JN

Proceedings of the National Academy of Sciences of the United States of America 19930901 18

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 ...[more]

PMID: 8378315

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