Supplemental Data
Files in this Data Supplement:
- Supplemental Figure 1 (.pdf, 1.6 MB) - Interactions among cytoplasmic dynein, LIS1, and NDEL1 fragments. A and B, The silver-stained gel images show that NC bound to dynein and NN did not. Sucrose gradients were divided into 19 fractions of equal volume. Sucrose concentration is indicated at the top. C, GST pull-down assay. The SDS-PAGE gel shows that NN bound to LIS1, but NC did not. GST-LIS1 was immobilized to GST-bind Resin (Novagen), and NDEL1 fragments were applied. The solutions were centrifuged using Micro Bio spin columns (Bio-Rad). The protein bound to GST-LIS1 was analyzed by SDS-PAGE. The Coomassie brilliant blue-stained gel shows that only NN bound to LIS1.
- Supplemental Figure 2 (.pdf, 4.4 MB) - Interactions between cytoplasmic dynein and GST-??N-LIS1/??N-LIS1. The silver-stained gel image shows that GST-??N-LIS1 (A) and ??N-LIS1 (B) bound to dynein. The sucrose gradients were divided into 16 fractions of equal volume. Sucrose concentration is indicated at the top.
- Supplemental Movie 5 (.mov, 252 KB) - The restoration of MT movement in the presence of both GST-??N-LIS1 and NN (3?~ Real Time). The movie shows that NN restored the gliding movement of MTs from the suppression by GST-??N-LIS1
- Supplemental Movie 1 (.mov, 1.6 MB) - The gliding movements of MTs over the dynein coated glass surface (3?~ Real Time).
- Supplemental Movie 4 (.mov, 167 KB) - The gliding movements of MTs in the presence of ??N-LIS1 (3?~ Real Time). The movie shows that ??N-LIS1 had little effect on the gliding movement of MTs
- Supplemental Movie 3 (.mov, 194 KB) - The suppression of MT movement in the presence of GST-??N-LIS1 (3?~ Real Time). The movie shows that GST-??N-LIS1 suppressed the gliding movement of MTs
- Supplemental Movie 2 (.mov, 3.9 MB) - The gliding movements of MTs in the presence of NC (3?~ Real Time). The movie shows that C-terminus fragment of NDEL1 facilitated the dissociation of dynein from MTs