Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery.

@article{Fernando2003PhosphorylationdependentSA,
  title={Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery.},
  author={Pasan Fernando and Lynn A. Megeney and John J. Heikkila},
  journal={Experimental cell research},
  year={2003},
  volume={286 2},
  pages={175-85}
}
Small heat shock proteins (hsps) act as molecular chaperones by preventing the thermal aggregation and unfolding of cellular protein; however, the manner by which cells regulate chaperone activity remains unclear. In the present study, we examined the role of phosphorylation on the chaperone function of the Xenopus small hsp30. Both heat stress and sodium arsenite treatment in A6 cells resulted in a rapid activation of p38alpha and MAPKAPK-2. Surprisingly, the association of MAPKAPK-2 with… CONTINUE READING