Figure 5: The N-BAR and SH3 domains of BIN1 have distinct roles in the recruitment of dynamin. | Nature Communications

Figure 5: The N-BAR and SH3 domains of BIN1 have distinct roles in the recruitment of dynamin.

From: BIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin

Figure 5

(a) Domain representation (N-BAR, PI domain and SH3 domain) of the full-length and N-BAR domain constructs used. Mutated amino acids in N-BAR D151N and stop codon in BIN1 SH3-ΔC are highlighted with a black star. (b) Binding kinetics of 0.3 μM dynamin to flat membranes containing 5% PtdIns(4,5)P2 in control conditions (dynamin alone) and in the presence of the constructs described in panel a. Data were fitted (solid lines) as described in Methods. (c) Binding of 0.3 μM dynamin to flat membranes containing 5% PtdIns(4,5)P2 in control conditions and in the presence of the constructs described in panel a. Measurements were performed from at least three independent experiments. Box plots display the average value (solid square, also shown on top of each box plot), the median value (solid line), the s.d. and the interquartile range (25–75%) (n=15, n=37, n=29, n=24, n=22 and n=31, for control, BIN1, Amphiphysin1, BIN1 SH3-ΔC, N-BAR, N-BAR D151N, respectively). Error bars represent s.d. **P<0.01, ***P<0.001 (t-test).

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