Title : The cytoplasmic tyrosine motifs in full-length glycoprotein 130 have different roles in IL-6 signal transduction.

Pub. Date : 2000 Jan 15

PMID : 10623831






6 Functional Relationships(s)
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1 The cytoplasmic tyrosine motifs in full-length glycoprotein 130 have different roles in IL-6 signal transduction. Tyrosine interleukin 6 signal transducer Mus musculus
2 However, the redundancy of the tyrosine motifs within the cytoplasmic part of gp130 has been neglected. Tyrosine interleukin 6 signal transducer Mus musculus
3 Here we describe the analysis of the function of the individual cytoplasmic tyrosine residues of gp130 in the context of the full-length receptor protein in IL-6 signaling as measured by STAT activation, acute phase protein induction, and stimulation of proliferation. Tyrosine interleukin 6 signal transducer Mus musculus
4 Our studies revealed that tyrosine motifs which have been described to recruit STAT proteins are not equivalent with respect to their potential to activate STAT factors and acute phase protein gene promoters: the two distal tyrosines, Tyr905 and Tyr915, of gp130 were more potent than Tyr767 and Tyr814. Tyrosine interleukin 6 signal transducer Mus musculus
5 Thus, the tyrosine residues in the cytoplasmic part of gp130 were found to contribute differentially to IL-6 signal transduction in the full- length gp130 protein. Tyrosine interleukin 6 signal transducer Mus musculus
6 Thus, the tyrosine residues in the cytoplasmic part of gp130 were found to contribute differentially to IL-6 signal transduction in the full- length gp130 protein. Tyrosine interleukin 6 signal transducer Mus musculus