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- _6 wasQuotedFrom 10851055 provenance.
- _6 value "Stat5 proteins activated by IL-2. The phosphorylated tyrosines on IL-2Rbeta can then serve as docking sites for signaling molecules that otherwise cannot associate with IL-2Rbeta, including the adaptor protein Shc, Stat5a, and Stat5b (Figure 2). For example, only phosphorylated (but not non-phosphorylated) peptides spanning either Tyr-392 or Tyr-510 of IL-2Rbeta can efficiently compete with IL-2-induced Stat5 DNA binding to a GAS motif IL-2-mediated hetero-dimerization of its receptor triggers a rapid increase in the recruitment of Jak3 and activation of both Jak1 and Jak3 (Johnston et al., 1994; Witthuhn et al., 1994). These kinases phosphorylate the receptor as well as each other, and activate other signaling molecules associated with the receptor. The phosphorylated tyrosines on IL-2Rbeta can then serve as docking sites for signaling molecules that otherwise cannot associate with IL-2Rbeta, including the adaptor protein Shc, Stat5a, and Stat5b" provenance.