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 Grb7?, 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.
Mesh Terms:
Animals, Calmodulin-Binding Proteins, Cell Cycle Proteins, Cell Line, Tumor, GRB7 Adaptor Protein, HEK293 Cells, HSC70 Heat-Shock Proteins, Humans, Mutation, Nedd4 Ubiquitin Protein Ligases, Protein Binding, Protein Domains, Protein Structure, Secondary, Proteomics, Rats
Animals, Calmodulin-Binding Proteins, Cell Cycle Proteins, Cell Line, Tumor, GRB7 Adaptor Protein, HEK293 Cells, HSC70 Heat-Shock Proteins, Humans, Mutation, Nedd4 Ubiquitin Protein Ligases, Protein Binding, Protein Domains, Protein Structure, Secondary, Proteomics, Rats
Arch Biochem Biophys
Date: Dec. 15, 2019
PubMed ID: 32360748
View in: Pubmed Google Scholar
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