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The Gα‐interacting vesicle‐associated protein interacts with and promotes cell surface localization of GRP78 during endoplasmic reticulum stress

Cell surface translocation of the chaperone glucose‐regulated protein 78 kDa (GRP78) is a key event that promotes cancer cell survival during endoplasmic reticulum (ER) stress. Here, we identify Gα‐interacting vesicle‐associated protein (GIV) – an enhancer of prosurvival signaling during ER stress – as a binding partner of GRP78. We show that GIV and GRP78 interact in an ER stress‐dependent manner through their respective carboxyl terminal domains and that GIV aids in the localization of GRP78 to the plasma membrane. Kaplan–Meier analysis of disease‐free survival in cancer patients shows poor prognosis for patients with high expression of both GIV and GRP78, further suggesting a vital role for these two proteins in enhancing cancer cell viability.