{"CAPTION FIG1.png": "'\\n\\n**Fig. 1 Knock-down of cortactin in MDA-MB-231 cells attenuates transferrin endocytosis**\\n\\n(A) Cortactin protein in siRNA treated cells was not detected by immunoblot assay. (B) Only about 50% of cells subjected to cortactin siRNA treatment. had normal transferrin (Tfri) uptake. (C) Tfri fluorescent intensity in cytoplasm in cortactin siRNA treated-cells was apparently reduced (lower panel, arrow head) in comparison to neighboring cells with relatively high cortactin levels (lower panel, arrow), or to mock-treated cells (upper panel). Magnification, 600\\\\(\\\\times\\\\).\\n\\n'", "CAPTION FIG2.png": "'\\n\\n**Fig. 2** **Introduction of coractin immunoreagents into live cells suppresses transferrin uptake**\\n\\nNIHGT3 cells were subjected to coractin immunoreagent infinduction mediated by the BioPORTER-resistance system. Quantitation of endocytic biotinylated-labeled transferrin (Tf) by ELISA-based transferrin uptake assay was performed 5 h after the start of the tratment. BioPORTER only (column 1)\\\\({}_{r}\\\\) rahit IgG (column 4) and labeled mouse IgG (column 5) with kit were used as control. Endocyteis is cells with either coctactin antibody (column 2) or 4F11 (column 3) was repaired.\\n\\n'", "CAPTION FIG3.png": "'\\n\\n**Fig. 3**: **Perturbation of actin dynamics by cytochalasin D affects the association of cortactin with dynamin at endocytosis sites** NIH/3T3 cells were treated with cytochalasin D in serum-free medium. The association of cortactin (red) with dynamin (green) was obvious in control cells without cytochalasin D treatment (A), and became invisible after cytochalasin D exposure (B), then was restored after the drug was washed out (C). Compared with the control (D), transferrin (green) endocytosis was reduced by cytochalasin D treatment for 1 h (E) and restored within 1 h after the drug was washed out (F). Magnification, 600x.\\n\\n'", "CAPTION FIG4.png": "'NH(3T 3 cells were seeded on fibronectin-coated coverslips the day before DNA transfection. Contraction was performed using Lipofectamine reagent. Red fluorescent protein (RFP)-contactin (A), dynamic-green fluorescent protein (GFP) (B) and AP-2 (C) co-distributed in cytoplasm and formed granular structure (D). In cells cotransfected with RFP-tagged wild-type outardin (E) and proline rich domain (PRD) depleted dynamin (F), the association of contraction with dynamin and AP-2 (G) was abolished (H). This phenomenon also happened in cells cotransfected with SH3 domain-deleted outardin and wild-type dynamin. Unlike wild-type outardin, RFP-ContASH3 (I) is not associated with dynamin (J) and AP-2 (K) any more, while the latter two still co-distributed in cytoplasm (L). In contactin SH3 domain only expressing cells, RFP-tagged outardin SH3 (M), GFP-tagged wild-type dynamin (N) and AP-2 (Q) were co-distributed as puncta-like structure in cytoplasm (P). When cells were cotransfected with coordinate SH3 and PRD-depleted dynamin, contactin SH3 domain (Q) lost its association with PRD-depleted dynamin (R) and AP-2 (S), while PRD-depleted dynamin (P-2 co-distribution was still present (T). Cells expressing RFP (U) and wild-type dynamin (V) were used as the control, no colocalization was found (X), and the colocalization between dynamin and AP-2 was not affected by GFP expression (W, X). Bars=10 \\\\(\\\\mu\\\\)m.\\n\\nFig. 4: In vivo recruitment of cortactin to endocytosis sites by dynamin'", "CAPTION FIG5.png": "'(A) Full-down assay of the interaction of GST-proline rich domain of dynamic and cortactin. (B) Purified contraction was mixed with different amounts of immobilized GST-tagged dynamic proline rich domain (Dyn PRD) protein. After incubation, samples were centrifuged (800 g) and the supernatants were collected for immunoblot assay to detect the amount of remaining cortactin with contractile antibody dF11. Amount of cortactin was quantified by digital scanning and normalized to the percentage of depletion. The resulting data were used to fit a rectangular hyperbola, yielding apparent _K_x values of 0.964 \u03bcM. (C) Fluorescent carboxylated polystyrene beads were coated with GST-Dyn-PRD by including beads in protein solution (5 mg/ml). Branched actin filaments were recruited to Dyn-PRD coated beads (a, b and c), but not to non-contact beads (d). Cort, cortactin. Magnification, 600%.\\n\\nFig. 5: Cortactin-mediated actin assembly is recruited to dynamin-coated beads in vitro (A) Full-down assay of the interaction of GST-proline rich domain of dynamic and cortactin. (B) Purified contraction was mixed with different amounts of immobilized GST-tagged dynamic proline rich domain (Dyn PRD) protein. After incubation, samples were centrifuged (800 g) and the supernatants were collected for immunoblot assay to detect the amount of remaining cortactin with contractile antibody dF11. Amount of cortactin was quantified by digital scanning and normalized to the percentage of depletion. The resulting data were used to fit a rectangular hyperbola, yielding apparent _K_x values of 0.964 \u03bcM. (C) Fluorescent carboxylated polystyrene beads were coated with GST-Dyn-PRD by including beads in protein solution (5 mg/ml). Branched actin filaments were recruited to Dyn-PRD coated beads (a, b and c), but not to non-contact beads (d). Cort, cortactin. Magnification, 600%.\\n\\n'", "CAPTION FIG6.png": "'\\n\\n**Fig. 6** **C ortactin functions in the late stage of clathrin coated vesicle (CCV) formation**\\n\\n(A) Western blot analysis of mtDNA cytosol before and after treatment with contractile antibody-coupled beads. Equivalent volumes of supernatants (lane 1 and lane 4) or beads after incubation (lane 5) and before incubation (lane 6), 1/2 loading volume (lane 2) and 1/4 loading volume of supernatants (lane 3) were probed with anti-contraction antibody 001. More than 95% cortactin was depleted (lane 4). (B) Permeabilized 3T3-L1 cells were incubated with mock-depleted cytosol (mock, column 1), cortactin, only (Cort, column 2), or cortactin-depleted cytosol (Cort D, column 3), or cortactin-depleted cytosol supplemented with recombinant cortactin SH3 domain (Cort D+Cort-SH3, column 4), N-terminal-depleted cortactin (Cort D+Cort-NTD, column 5) or wild-type contraction (Cort D+Cort, column 6). Endocytosis was measured by MetaNa resistance in specially detect internalization of B-SS-transferrin (Tfru) into sealed vesicles.\\n\\n'"}