The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart.

@article{Scholz2001TheMC,
  title={The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart.},
  author={Glen M Scholz and Steven D. Hartson and Kellie Cartledge and Lenora Volk and Robert L. Matts and Ashley R. Dunn},
  journal={Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research},
  year={2001},
  volume={12 8},
  pages={
          409-17
        }
}
We have investigated the relationship between the molecular chaperone heat shock protein-90 (Hsp90) and the signal transducing capacity of the Src-family kinase Hck. Inhibition of Hsp90 with geldanamycin suppressed the ability of bacterial lipopolysaccharide to enhance the cell adhesion properties of macrophages, a phenomenon most likely explained by the reduced expression and activity of Hck in macrophages lacking Hsp90 function. The contribution of Hsp90 to signal transduction by Hck was… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-8 OF 8 CITATIONS

Contribution of chaperones to STAT pathway signaling.

VIEW 5 EXCERPTS
CITES BACKGROUND, RESULTS & METHODS
HIGHLY INFLUENCED