Gene interactions and pathways from curated databases and text-mining
Biochem Biophys Res Commun 2003, PMID: 12559950

Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3.

Sato, Noriko; Yamamoto, Tetsuya; Sekine, Yuichi; Yumioka, Taro; Junicho, Akira; Fuse, Hideki; Matsuda, Tadashi

Interleukin-6 (IL-6) is a multifunctional cytokine playing roles in the immune system, hematopoiesis, and acute phase reactions. IL-6 also regulates the growth of various types of human malignant tumors. Here we demonstrate that IL-6-induced gene expression was suppressed by a specific heat-shock protein 90 (Hsp90) inhibitor, geldanamycin (GA) in human hepatoma Hep3B cells. GA also suppressed the IL-6-induced activation of signal transducer and activator of transcription 3 (STAT3) in a human embryonic kidney carcinoma 293T cells. This inhibitory effect of GA on STAT3 activation was reversed by overexpression of Hsp90. Furthermore, Hsp90 directly bound to STAT3 via its N-terminal region, which interacted with GA. We provide evidence that the action of GA on IL-6 functions was due to the inhibition of direct physical interactions between STAT3 and Hsp90, which represents a novel role of Hsp90 in the IL-6 signaling pathways.

Document information provided by NCBI PubMed

Text Mining Data

Dashed line = No text mining data

Manually curated Databases

  • IRef Biogrid Interaction: STAT3 — HSP90AA1 (physical association, affinity chromatography technology)
  • IRef Hprd Interaction: STAT3 — HSP90AB1 (in vivo)
  • IRef Hprd Interaction: STAT3 — HSP90AA1 (in vivo)
  • IRef Ophid Interaction: STAT3 — HSP90AB1 (aggregation, confirmational text mining)
  • IRef Ophid Interaction: STAT3 — HSP90AA1 (aggregation, confirmational text mining)
In total, 2 gene pairs are associated to this article in curated databases