BLTP2 interacts with amphiphysin 2 in an SH3 domain–dependent manner. (A–C) A 3 μm line was drawn onto BLTP2-positive tubules in a peripheral (portion positive for BAR protein only) to center direction. The intensity profile of both BLTP2^Halo and the BAR domain proteins are shown. n = 25 tubules for each experiment. Corresponding to Fig. 6, G–I. Mean ± SEM. (D) COS-7 cells showing that BLTP2^Halo is recruited to PM tubular invaginations induced by expression of CFP-mAmph2. (E) COS-7 cells showing that BLTP2^Halo is not recruited to PM tubular invaginations induced by expression of GFP-mAmph2 BAR*, which lacks the SH3 domain. (F) COS-7 cells showing that BLTP2^Halo is not recruited to PM tubular invaginations induced by expression of GFP-FBP17. (G) Sequence alignment of the region comprising the RAPHPP motif among BLTP2 from several organisms. The RAPHPP motif is conserved among mammalian species (blue arrowhead).
Figure S4.

BLTP2 interacts with amphiphysin 2 in an SH3 domain–dependent manner. (A–C) A 3 μm line was drawn onto BLTP2-positive tubules in a peripheral (portion positive for BAR protein only) to center direction. The intensity profile of both BLTP2^Halo and the BAR domain proteins are shown. n = 25 tubules for each experiment. Corresponding to Fig. 6, G–I. Mean ± SEM. (D) COS-7 cells showing that BLTP2^Halo is recruited to PM tubular invaginations induced by expression of CFP-mAmph2. (E) COS-7 cells showing that BLTP2^Halo is not recruited to PM tubular invaginations induced by expression of GFP-mAmph2 BAR*, which lacks the SH3 domain. (F) COS-7 cells showing that BLTP2^Halo is not recruited to PM tubular invaginations induced by expression of GFP-FBP17. (G) Sequence alignment of the region comprising the RAPHPP motif among BLTP2 from several organisms. The RAPHPP motif is conserved among mammalian species (blue arrowhead).

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