Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology

@article{Kostenko2009HeatSP,
  title={Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology},
  author={Sergiy Kostenko and Ugo Moens},
  journal={Cellular and Molecular Life Sciences},
  year={2009},
  volume={66},
  pages={3289-3307}
}
The small heat shock protein Hsp27 or its murine homologue Hsp25 acts as an ATP-independent chaperone in protein folding, but is also implicated in architecture of the cytoskeleton, cell migration, metabolism, cell survival, growth/differentiation, mRNA stabilization, and tumor progression. A variety of stimuli induce phosphorylation of serine residues 15, 78, and 82 in Hsp27 and serines 15 and 86 in Hsp25. This post-translational modification affects some of the cellular functions of Hsp25/27… CONTINUE READING