Interaction of BAG1 and Hsp70 mediates neuroprotectivity and increases chaperone activity

2005 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​Interaction of BAG1 and Hsp70 mediates neuroprotectivity and increases chaperone activity​
Liman, J. ; Ganesan, S.; Dohm, C. P. ; Krajewski, S.; Reed, J. C.; Bähr, M.   & Wouters, F. S.  et al.​ (2005) 
Molecular and Cellular Biology25(9) pp. 3715​-3725​.​ DOI: 

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Liman, Jan ; Ganesan, Sundar; Dohm, Christoph Peter ; Krajewski, S.; Reed, John C.; Bähr, Mathias ; Wouters, Fred S. ; Kermer, Pawel 
It was recently shown that Bcl-2-associated athanogene 1 (BAG1) is a potent neuroprotectant as well as a marker of neuronal differentiation. Since there appears to exist an equilibrium within the cell between BAG1 binding to heat shock protein 70 (Hsp70) and BAG1 binding to Raf-1 kinase, we hypothesized that changing BAG1 binding characteristics might significantly alter BAG1 function. To this end, we compared rat CSM14.1 cells and human SHSY-5Y cells stably overexpressing full-length BAG1 or a deletion mutant (BAG Delta C) no longer capable of binding to Hsp70. Using a novel yellow fluorescent protein-based foldase biosensor, we demonstrated an upregulation of chaperone in situ activity in cells overexpressing full-length BAG1 but not in cells overexpressing BAG Delta C compared to wild-type cells. Interestingly, in contrast to the nuclear and cytosolic localizations of full-length BAG1, BAG Delta C was expressed exclusively in the cytosol. Furthermore, cells expressing BAG Delta C were no longer protected against cell death. However, they still showed accelerated neuronal differentiation. Together, these results suggest that BAG1-induced activation of Hsp70 is important for neuroprotectivity, while BAG1-dependent modulation of neuronal differentiation in vitro is not.
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Molecular and Cellular Biology 



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