Title : Activation of JAK2 kinase mediated by the interleukin 6 signal transducer gp130.

Pub. Date : 1994 Mar 15

PMID : 8134389






3 Functional Relationships(s)
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1 We show here that JAK2 kinase is rapidly tyrosine phosphorylated in mouse embryonic stem cells whose pluripotentiality is maintained only by gp130-sharing cytokines after stimulation that is known to induce gp130 homodimerization. Tyrosine interleukin 6 signal transducer Mus musculus
2 Deletion or point mutation in the membrane-proximal cytoplasmic motifs in gp130 that are conserved in the hemopoietic cytokine receptor family results in the loss of tyrosine phosphorylation of JAK2, which coincides with the lack of signal transducing capability of gp130 mutants. Tyrosine interleukin 6 signal transducer Mus musculus
3 Deletion or point mutation in the membrane-proximal cytoplasmic motifs in gp130 that are conserved in the hemopoietic cytokine receptor family results in the loss of tyrosine phosphorylation of JAK2, which coincides with the lack of signal transducing capability of gp130 mutants. Tyrosine interleukin 6 signal transducer Mus musculus