Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth.
BAG-1, a multifunctional protein, interacts with a plethora of cellular targets where the interaction with HSC70 and HSP70, is considered vital. Structural studies have demonstrated the C-terminal of BAG-1 forms a bundle of three alpha-helices of which helices 2 and 3 are directly involved in binding to the chaperones. Here ... we found peptides derived from helices 2 and 3 of BAG-1 interfered with BAG-1:HSC70 binding. We confirmed that a 12 amino-acid peptide from helix 2 directly interacted with HSC70 and when introduced into MCF-7 and ZR-75-1 cells, these peptides inhibited their growth. In conclusion, we have identified a small domain within BAG-1 which appears to play a critical role in the interaction with HSC70.
Mesh Terms:
Amino Acid Sequence, Breast Neoplasms, Cell Line, Tumor, Cell Proliferation, DNA-Binding Proteins, HSC70 Heat-Shock Proteins, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Peptide Fragments, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Surface Plasmon Resonance, Transcription Factors
Amino Acid Sequence, Breast Neoplasms, Cell Line, Tumor, Cell Proliferation, DNA-Binding Proteins, HSC70 Heat-Shock Proteins, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Peptide Fragments, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Surface Plasmon Resonance, Transcription Factors
FEBS Lett.
Date: Nov. 03, 2009
PubMed ID: 19800331
View in: Pubmed Google Scholar
Download Curated Data For This Publication
154913
Switch View:
- Interactions 2