Stress-induced translocation of the endoplasmic reticulum chaperone GRP78/BiP and its impact on human disease and therapy.

ABSTRACT: Since their discoveries in the 1960s as a family of proteins produced by cells in response to stress, molecular chaperones are increasingly recognized as major regulators of cellular homeostasis in health and disease. Among the heat shock protein 70 family, the 78-kDa glucose-regulated protein (GRP78), also referred to as BiP and encoded by the HSPA5 gene, contains a signal peptide targeting it into the endoplasmic reticulum (ER). Through its interaction with the transmembrane ER stress sensors, GRP78 acts as a master regulator of the Unfolded Protein Response (UPR) which allows cells to adapt to stress observed in many human diseases. The discovery that ER stress not only upregulates GRP78 to cope with ER protein quality control but also actively promotes its relocation to other ce

SUBMITTER: Lee AS 

PROVIDER: S-EPMC12318151 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature