Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat-shock protein 27.

@article{Landry1995ModulationOA,
  title={Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat-shock protein 27.},
  author={Jacques Landry and Jacques Huot},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={1995},
  volume={73 9-10},
  pages={
          703-7
        }
}
HSP27, like other proteins of the heat-shock protein family, accumulates to high levels after exposure of cells to a short period of hyperthermia and contributes to the development of a transient state of thermoresistance. In vitro, HSP27 behaves as an actin cap-binding protein and can inhibit actin polymerization. In vivo, the protective function of HSP27 is exerted mainly at the level of the microfilaments and appears as an extension of a normal function of the protein. This function is… CONTINUE READING
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