Skip to main content
. 2006 Oct;17(10):4564–4575. doi: 10.1091/mbc.E05-10-0994

Figure 2.

Figure 2.

DdWIPa is structurally and functionally similar to mammalian Wasp Interacting Protein (WIP). (A) Schematic representations of mammalian WIP and Dictyostelium WIPa. Sequence alignment of Wasp Homology 2 (WH2) domain shown with conserved residues in black. Residues essential for binding to G-actin are indicated with asterisks. Lysine 36 is indicated with an arrow. (B) YFP-WIPa was precipitated from AX3 cell lysates with either GST-fusion wild type or mutant WH1 bound to glutathione beads. Representative of three experiments is shown. IB, immunoblot; C, Coomassie staining. (C) Purified His-tagged WIPa was pulled down from solution using GST-WH1 or -WASP bound to beads. Representative of three experiments is shown. Each pulldown was quantitated and normalized to the quantity of GST-tagged protein used in the experiment. (D) Interaction between WH1 domain and WIPa depends partially on conserved residues K93 and S95 of WIPa. Purified His-tagged WT or mutant KS WIPa was pulled down from solution using GST-WH1. Three representative experiments are shown.