HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation.

@article{Parcellier2003HSP27IA,
  title={HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation.},
  author={Arnaud Parcellier and Elise Schmitt and Sandeep Gurbuxani and Daphn{\'e} Seigneurin-Berny and Alena Pance and Aur{\'e}lie Chant{\^o}me and St{\'e}phanie Plenchette and Saadi Khochbin and {\'E}ric Solary and Carmen Garrido},
  journal={Molecular and cellular biology},
  year={2003},
  volume={23 16},
  pages={5790-802}
}
HSP27 is an ATP-independent chaperone that confers protection against apoptosis through various mechanisms, including a direct interaction with cytochrome c. Here we show that HSP27 overexpression in various cell types enhances the degradation of ubiquitinated proteins by the 26S proteasome in response to stressful stimuli, such as etoposide or tumor necrosis factor alpha (TNF-alpha). We demonstrate that HSP27 binds to polyubiquitin chains and to the 26S proteasome in vitro and in vivo. The… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 112 extracted citations

Interactions of the proteasomal system with chaperones: protein triage and protein quality control.

Progress in molecular biology and translational science • 2012
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…