Interleukin-6 induces tyrosine phosphorylation of the Ras activating protein Shc, and its complex formation with Grb2 in the human multiple myeloma cell line LP-1
✍ Scribed by Carola Neumann; Gundula Zehentmaier; Susanne Danhauser-Riedl; Bertold Emmerich; Michael Hallek
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 701 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0014-2980
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✦ Synopsis
Interleukin-6 induces tyrosine phosphorylation of the Ras activating protein Shc, and its complex formation with Grb2 in the human multiple myeloma cell line LP-1
Like many other cytokines and growth factors, interleukin-6 (IL-6) activates ~21'"'. However, the precise biochemical mechanisms inducing this activation are unknown. Therefore, we investigated the effects of IL-6 on some recently identified signaling intermediates, Shc (Src homology and collagen) and Grb2 (growth factor receptor bound protein 2), known to activate ~21'"'. In the multiple myeloma cell line LP-1, IL-6 stimulated the tyrosine phosphorylation of Shc in a time-and concentration-dependent manner. This led to the complex formation of Shc with Grb2, an adaptor protein known to relocate a p2lraS-GDP exchange factor, Sosl (Son-of-sevenless), to the cell membrane. Taken together, these findings suggest that IL-6 might activate the Ras signaling pathway via tyrosine phosphorylation of Shc and subsequent recruitment of Grb2. Further studies will elucidate which of the IL-6 receptor associated non-receptor tyrosine kinases of the Src kinase or Janus kinase family, mediate these effects.