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小鼠Jak2蛋白酪氨酸激酶的结构及其在白细胞介素3信号转导中的作用。

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

作者信息

Silvennoinen O, Witthuhn B A, Quelle F W, Cleveland J L, Yi T, Ihle J N

机构信息

Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, TN 38105.

出版信息

Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8429-33. doi: 10.1073/pnas.90.18.8429.

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.

摘要

白细胞介素3(IL-3)调节造血细胞的增殖和分化。尽管IL-3受体链缺乏激酶催化结构域,但IL-3可诱导细胞蛋白的酪氨酸磷酸化。为了研究蛋白酪氨酸激酶JAK家族在IL-3信号转导中的潜在作用,我们获得了小鼠Jak1和Jak2蛋白酪氨酸激酶的全长cDNA克隆,并制备了针对预测蛋白的抗血清。使用抗Jak2的抗血清,我们证明IL-3刺激导致Jak2快速且特异性的酪氨酸磷酸化,并激活其体外激酶活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6544/47370/aaaeb128e8fd/pnas01475-0135-a.jpg

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