Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27.

@article{Lavoie1995ModulationOC,
  title={Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27.},
  author={Jos{\'e}e N. Lavoie and Herman Lambert and Eileen Hickey and Lilian A. E. Weber and Jean-François. Landry},
  journal={Molecular and cellular biology},
  year={1995},
  volume={15 1},
  pages={
          505-16
        }
}
Phosphorylation of heat shock protein 27 (HSP27) can modulate actin filament dynamics in response to growth factors. During heat shock, HSP27 is phosphorylated at the same sites and by the same protein kinase as during mitogenic stimulation. This suggests that the same function of the protein may be activated during growth factor stimulation and the stress response. To determine the role of HSP27 phosphorylation in the heat shock response, several stable Chinese hamster cell lines that… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 212 CITATIONS, ESTIMATED Infinity% COVERAGE

212 Citations

01020'96'01'07'13'19
Citations per Year
Semantic Scholar estimates that this publication has 212 citations based on the available data.

See our FAQ for additional information.

Similar Papers

Loading similar papers…