Figure 2.
TPD54 directly associates with liposomes in vitro.(A) Cosedimentation of GST, GST-TPD54 WT, or GST-TPD54 mutants as indicated with differently sized liposomes (diameter indicated) or no liposomes (−), visualized on an InstantBlue-stained 4% to 12% gel. S, supernatant; P, pellet. (B) Pelleting of differently sized liposomes visualized on a Coomassie-stained Bis-Tris gel showing lipid stain. (C) Quantification of the pelleting efficiency of liposomes according to their size. Values are normalized to 100 nm liposomes. Points show mean ± SD; n = 3. (D) Quantification of protein cosedimentation with differently sized liposomes. The binding of GST (dark gray), GST-TPD54 (WT, blue), or GST-TPD54 (1–82, light gray) is shown relative to TPD54 binding to 100 nm. (E) Quantification as in D, but with all mutants overlaid. Points show mean ± SEM; n = 3, except n = 6 for GST, TPD54, and R159E.

TPD54 directly associates with liposomes in vitro. (A) Cosedimentation of GST, GST-TPD54 WT, or GST-TPD54 mutants as indicated with differently sized liposomes (diameter indicated) or no liposomes (−), visualized on an InstantBlue-stained 4% to 12% gel. S, supernatant; P, pellet. (B) Pelleting of differently sized liposomes visualized on a Coomassie-stained Bis-Tris gel showing lipid stain. (C) Quantification of the pelleting efficiency of liposomes according to their size. Values are normalized to 100 nm liposomes. Points show mean ± SD; n = 3. (D) Quantification of protein cosedimentation with differently sized liposomes. The binding of GST (dark gray), GST-TPD54 (WT, blue), or GST-TPD54 (1–82, light gray) is shown relative to TPD54 binding to 100 nm. (E) Quantification as in D, but with all mutants overlaid. Points show mean ± SEM; n = 3, except n = 6 for GST, TPD54, and R159E.

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