Figure 1
Figure 1. PU-H71 association-based identification of proteins involved in NF-κB activation, apoptosis, and autophagy in PEL cells. (A) PU-H71 affinity capture of BC3 cell extracts was followed by proteomic analysis. Proteins identified in these pull-downs are as follows: those involved in NF-κB signaling are blue; those involved in apoptosis are green; and ATG3, involved in autophagy, is brown. vFLIP, a key nodal protein, is shown in orange. Results shown are from 1 of 2 independent experiments. (B) Immunoblot from PU-H71 pull-downs, but not control bead pull-downs, using extracts from the indicated cell lines, confirmed that Hsp90 interacts with selected proteins in key pathways, including NF-κB (p65), apoptosis (MCL1, cIAP1), and autophagy (ATG3).

PU-H71 association-based identification of proteins involved in NF-κB activation, apoptosis, and autophagy in PEL cells. (A) PU-H71 affinity capture of BC3 cell extracts was followed by proteomic analysis. Proteins identified in these pull-downs are as follows: those involved in NF-κB signaling are blue; those involved in apoptosis are green; and ATG3, involved in autophagy, is brown. vFLIP, a key nodal protein, is shown in orange. Results shown are from 1 of 2 independent experiments. (B) Immunoblot from PU-H71 pull-downs, but not control bead pull-downs, using extracts from the indicated cell lines, confirmed that Hsp90 interacts with selected proteins in key pathways, including NF-κB (p65), apoptosis (MCL1, cIAP1), and autophagy (ATG3).

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