{"CAPTION FIG1-1.png": "'Figure 2: The BAR and FH Domaire Localize GRAF1 to Highly Curved, Plains(4,5)P2-Zeninched Membranes, and the SH3 Domain Binds Dynamic (A) Coomassie-stained gel of liposome cosedimentation assay showing the preference of GST-tagged GRAF1 BAR+PH protein for binding to smaller-sized liposomes derived from total brain lipids (the average diameters of liposomes are shown). Pellet (P) and supernatant (S) fractions were separated by ultra-centrifugation. The graph shows quantifications of total band intensities for each condition normalized to binding of the non-curvature-sensitive protein Dah2 (as a way of controlling for total lipid in each experiment). The error bars show 95% confidence intervals (calculated by t) tests for each condition. (B) Liposome cosedimentation assay as performed in (A) but with 0.8-\u03bcm-diameter liposomes enriched with varying phospholipids. (C) Electron micrographs of negatively stained liposomes incubated in the presence or absence of GST-tagged GRAF1 BAR+PH protein. Note the protein-dependent presence of tubular structures. The scale bar represents 200 nm. (D) Immunoprecipitation of GRAF1 from rat brain cytosol (via Ab2) reveals a GRAF1-Dynamim1 complex as identified by mass spectrometry and confirmed by immunoblot. (E) Coomassie-stained gels of pull-down experiments with purified Dynamim and either bead-bound GST-tagged GRAF1/Amphighysin SH3 domain or GRAF1 BAR+PH protein. P = pellet fraction, S = supernatant fraction. (F and G) Epifluorescence micrographs of HeLa cell overexpressing Myc-tagged GRAF1 and incubated with CT&B for 5 min before fixation and staining. (G) Epifluorescence micrographs of a HeLa cellincubated with CT&B for 5 min before fixation and staining for endogenous GRAF1. Scale bars represent 10 \u03bcm.\\n\\n'", "CAPTION FIG4.png": "'Figure 4: GRAF1 Is Indispensable for Ciaithrin-Independent Fluid-Phase Uptake in Fibroblasts (A) Immunoblots on HeLa cell lysates transfected with a control siRNA or either of two siRNAs directed against GRAF1 mRNA (siRNA a and b). Detection of GRAF1 and tubulin (loading control) was performed with specific antibodies on lysates obtained 48 hr after transfection. (B) GRAF1-depleted cells show a major reduction in fluid-phase endocytosis as shown by the decrease in the uptake of FITC-labeled dextran (control siRNA \\\\(n\\\\) = 5), siRNA (\\\\(n\\\\) = 8), or APE siRNA (\\\\(n\\\\) = 3). The error bars show the standard deviation of the mean. (C and D) HeLa cells depleted of GRAF1 were incubated with dextran (C) or transferrin (D) for 15 min before fixation and staining. Scale bars represent 10 \\\\(\\\\mu\\\\)m.\\n\\n'", "CAPTION FIG1-2.png": "'\\n\\n**(G) Electron micrographs prepared as described and immunolabeled for GRAF1 (10 nm gold particles). Note the GRAF1-positive tubular structures. Distance between arrowhead tips = 40 nm. Scale bars represent 10 \u03bcm.**'", "CAPTION FIG3.png": "'Figure 3: GRAF1 Regulates the CLIC Endocylic Pathway (A) Representative electron micrographs of 65 nm ultrathin cryosections of HeLa cells transiently transfected with GFP-GPI alone or with both GFP-GPI and Myc-tagged GRAF1 FL. Cells were fixed in 2% PFA with 0.2% glutaraldehyde and labeled with anti-GFP and anti-_Myc_ antibodies. Protein A 10 nm gold was used for revealing the GFP in the single labeling (upper image). As shown, GFP-GPI was found in uncoated vesicles and tubules within the cell. Double labeling of GRAF1 (Protein A gold 10 nm) and GFP-GPI (Protein A gold 15 nm) is shown in the bottom image, where colocalization of GRAF1 and GFP-GPI is seen in an intracellular tubule. Arrowheads point to 10 nm gold particles. Due to limitations of the \\n\\n'", "CAPTION FIG1.png": "'\\n\\n## References\\n\\n* [1] A. A. K. K.\\n\\n'"}