Figure S2.
Oligomerization status of IRSp53 constructs in solution. (A) miniDawn analysis showing that the full-length IRSp53 exists as a dimer at 100 μM in solution. Superose 6 increase column was used for size-exclusion chromatography. Calculated MW of IRSp53 is 57.4 kD. (B) miniDawn analysis showing IRSp53 becomes monomeric after removal of the BAR domain; replacement of the BAR with a dimeric coiled coil from myosin X could restore its oligomerization. Superose 12 10/300 column was used for size-exclusion chromatography. Analysis was performed at 100 μM protein concentration. Calculated MW of IRSp53_ΔBAR is 28.5 kD, and that of Myo-CC+ΔBAR is 34.4 kD.

Oligomerization status of IRSp53 constructs in solution. (A) miniDawn analysis showing that the full-length IRSp53 exists as a dimer at 100 μM in solution. Superose 6 increase column was used for size-exclusion chromatography. Calculated MW of IRSp53 is 57.4 kD. (B) miniDawn analysis showing IRSp53 becomes monomeric after removal of the BAR domain; replacement of the BAR with a dimeric coiled coil from myosin X could restore its oligomerization. Superose 12 10/300 column was used for size-exclusion chromatography. Analysis was performed at 100 μM protein concentration. Calculated MW of IRSp53_ΔBAR is 28.5 kD, and that of Myo-CC+ΔBAR is 34.4 kD.

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