Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin‐6

FEBS Letters

Hibi, Masahiko¹  Liu, Yin¹  Kishimoto, Tadamitsu²  Taga, Tetsuya¹  Narazaki, Masashi¹  Lee, Ihn-Sook¹ 

[1] Institute for Molecular and Cellular Biology, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565, Japan;Department of Medicine III, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565, Japan

关键词: Signal transduction;    Tyrosine phosphorylation;    Vav;    gp130;    IL;    interleukin;    MAPK;    mitogen-activated protein kinase;    Erk2;    extracellular signal-regulated kinase 2;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(96)01456-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Vav is a hematopoietic cell-specific proto-oncogene. We show that interleukin-6 (IL-6) induces transient tyrosine phosphorylation of Vav in a human myeloma cell line, U266. A membrane-distal part of the cytoplasmic region of gp130 is critical for association between Vav and gp130, and the IL-6-induced tyrosine phosphorylation of Vav. Mitogen-activated protein kinase (MAPK) (p42^MAPK or extracellular signal-regulated kinase 2 (Erk2)) is coprecipitated with Vav. MAPK activity in the anti-Vav immunoprecipitates is upregulated by IL-6 stimulation. Furthermore Vav is associated with Grb2 which is known as an adapter protein leading to Ras activation. The results imply that Vav may link gp130 activation to downstream MAPK activation in hematopoietic cells.

【 授权许可】

Unknown