The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.

@article{Behnke2014TheLH,
  title={The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.},
  author={Julia Behnke and Linda M Hendershot},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 5},
  pages={2899-907}
}
The Hsp70 superfamily is a ubiquitous chaperone class that includes conventional and large Hsp70s. BiP is the only conventional Hsp70 in the endoplasmic reticulum (ER) whose functions include: assisting protein folding, targeting misfolded proteins for degradation, and regulating the transducers of the unfolded protein response. The ER also possesses a single large Hsp70, the glucose-regulated protein of 170 kDa (Grp170). Like BiP it is an essential protein, but its cellular functions are not… CONTINUE READING
18 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 18 extracted citations

Similar Papers

Loading similar papers…