Abstract
Glycoprotein 96 (gp96) is a member of the heat shock protein 90 family, which is an ubiquitous family of molecular chaperones that are involved in the regulation of protein folding and other essential cellular activities. Residing in the lumen of the endoplasmic reticulum, gp96 plays a key role in maintaining protein homeostasis, from assemblage to degradation. However, exposure to stressful conditions that disturb cellular homeostasis may translocate gp96 to the cell surface, which implies its additional functions, such as the regulation of intracellular signalling, proliferation, and apoptosis, as well as the modulation of the immune response. Besides its roles under physiological conditions, gp96 is also included in different stages of oncogenesis. In this review, we summarised available data on the structure, physiological, and pathophysiological roles of gp96, particularly in breast cancer oncogenesis.
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