Fig. 2: Single alanine mutations of the 113-116 nexus cause BAX autoactivation and membrane poration. | Nature Communications

Fig. 2: Single alanine mutations of the 113-116 nexus cause BAX autoactivation and membrane poration.

From: The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core

Fig. 2

a–e SEC profiles of full-length, recombinant wild-type (a), L113A (b), F114A (c), Y115A (d), and F116A (e) BAX proteins (5 μM). SEC experiments were repeated twice using independent preparations of protein with similar results. f–j Liposomal release of ANTS/DPX by wild-type (f), L113A (g), F114A (h), Y115A (i), and F116A (j) BAX proteins (500 nM) in the presence and absence of the BH3-only activator tBID (10 nM). (k) Control experiment documenting the capacity of BCL-XLΔC (10 μM) to inhibit tBID-induced, BAX-mediated liposomal release, whereas G138A point mutagenesis blocks the inhibitory activity of BCL-XLΔC. l–o Effect of BCL-XLΔC and BCL-XLΔC G138A (10 μM) on the liposomal release autoactivity of L113A (l), F114A (m), Y115A (n), and F116A (o) BAX proteins (500 nM). Data are mean ± s.e.m. for liposomal release assays performed in technical quadruplicate and conducted twice using independent preparations of liposomes and proteins with similar results. Source Data are provided as a Source Data File.

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