[HTML][HTML] Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP
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. Here we report that ER stress actively promotes …
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. Here we report that ER stress actively promotes …
