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Files in this Data Supplement:
Table S1. Summary of one-way ANOVA analysis of kymographic data (see Fig. 2 and Materials and methods for further details).
Fig. S1. IQGAP1ΔNT does not bind F-actin. Polymerized actin, full-length IQGAP1 and IQGAP1ΔNT were centrifuged at low speed individually and in the indicated combinations, and the supernatants (S) and pellets (P) were analyzed by SDS-PAGE. Under these conditions, neither full-length IQGAP1 nor IQGAP1ΔNT pelleted, and only a small fraction of the F-actin pelleted in the absence of other proteins. Most F-actin pelleted in the presence of full-length IQGAP1, because IQGAP1 bound and crosslinked actin filaments into more readily sedimentable aggregates. By contrast, the amount of sedimentable F-actin was not increased by the presence of IQGAP1ΔNT, because IQGAP1ΔNT was unable to bind and crosslink actin filaments.
Movie 1. IQGAP1-stimulated assembly of branched actin filament networks observed directly by TIRF microscopy. The movie corresponds to Figure 5C-E.
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