Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth |
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| Authors: | Adam Sharp Peter WM Johnson Paul A Townsend |
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| Institution: | a Cancer Research UK Centre, Cancer Sciences Division, University of Southampton, School of Medicine, Southampton General Hospital, Southampton S016 6YD, UK
b Human Genetics Division, University of Southampton, School of Medicine, Southampton General Hospital, Southampton S016 6YD, UK |
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| Abstract: | 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.Structured summaryMINT-7265269, MINT-7265296, MINT-7265324, MINT-7265339, MINT-7265351, MINT-7265364, MINT-7265483, MINT-7265464, MINT-7265310: HSC70 (uniprotkb:P11142) binds (MI:0407) to BAG1 (uniprotkb:Q99933) by peptide array (MI:0081)MINT-7265281: peptide 15L (uniprotkb:Q99933) binds (MI:0407) to HSC70 (uniprotkb:P11142) by surface plasmon resonance (MI:0107) |
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| Keywords: | BAG bcl2-associated athanogene-1 HSC70 heat shock cognate 70 HSP70 heat shock protein 70 SPR surface plasmon resonance |
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