Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP.

@article{Zhang2010CellSR,
  title={Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP.},
  author={Yi Irvette Zhang and Ren Liu and Min Ni and Parkash Gill and Amy Si-Ying Lee},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 20},
  pages={15065-75}
}
The recent discovery that GRP78/BiP, a typical endoplasmic reticulum (ER) lumenal chaperone, can be expressed on the cell surface, interacting with an increasing repertoire of surface proteins and acting as receptor in signaling pathways, represents a paradigm shift in its biological function. However, the mechanism of GRP78 trafficking from the ER to the cell surface is not well understood. Using a combination of cellular, biochemical, and mutational approaches, we tested multiple hypotheses… CONTINUE READING