Partners of wild type Grb7 and a mutant lacking its calmodulin-binding domain

Irene García-Palmero, Neelam Shah, Naveid A. Ali, Roger J. Daly, Jacqueline A. Wilce, Antonio Villalobo

Research output: Contribution to journalArticleResearchpeer-review


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 Grb7Δ, 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.

Original languageEnglish
Article number108386
Number of pages8
JournalArchives of Biochemistry and Biophysics
Publication statusPublished - 15 Jul 2020


  • Calmodulin
  • Caprin-1
  • Grb7
  • Hsc70
  • Nedd4
  • Proteomics

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