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Updated: Jan 3, 2026

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
Published on: May 21, 2014
The Gα-interacting vesicle-associated protein interacts with and promotes cell surface localization of GRP78 during
Clariss Limso1, Jordan Matthew Ngo1, Peter Nguyen1
1Department of Chemistry and Biochemistry, California State University Long Beach, CA, USA.
Abstract:
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.
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