a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells.. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Note: This description may include information from UniProtKB.
Molecular Function: ATPase activity; calcium ion binding; chaperone binding; enzyme binding; glycoprotein binding; misfolded protein binding; protein binding; protein domain specific binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: cellular response to glucose starvation; ER-associated protein catabolic process; negative regulation of apoptosis; positive regulation of cell migration; substantia nigra development; unfolded protein response