Partners of wild type Grb7 and a mutant lacking its calmodulin-binding domain
Growth factor receptor bound protein 7 (Grb7) is a mammalian adaptor protein participating in signaling pathways implicated in cell migration, metastatic invasion, cell proliferation and tumor-associated angiogenesis. We expressed tagged versions of wild type Grb7 and the mutant Grb7Delta, lacking its calmodulin-binding domain (CaM-BD), in human embryonic kidney (HEK) 293 cells and rat glioma C6 cells to identify novel binding partners using shot-gun proteomics. Among the new identified proteins, we validated the ubiquitin-ligase Nedd4 (neural precursor cell expressed developmentally down-regulated protein 4), the heat-shock protein Hsc70/HSPA8 (heat shock cognate protein 70) and the cell cycle regulatory protein caprin-1 (cytoplasmic activation/proliferation-associated protein 1) in rat glioma C6 cells. Our results suggest a role of Grb7 in pathways where these proteins are implicated. These include protein trafficking and degradation, stress-response, chaperone-mediated autophagy, apoptosis and cell proliferation.
|ISBN||1096-0384 (Electronic) 0003-9861 (Linking)|
|Authors||Garcia-Palmero, I.; Shah, N.; Ali, N. A.; Daly, R. J.; Wilce, J. A.; Villalobo, A.|
|Publisher Name||ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS|
|URL link to publisher's version||https://www.ncbi.nlm.nih.gov/pubmed/32360748|