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Figure 7. The BR in the NH2 terminus of N-WASP specifically binds to PI(4,5)P2. (A) Diagram showing various mutants of the GBR of bovine N-WASP, which includes the BR and the Cdc42/Rac interactive binding (CRIB) motif. In GBR4, the four Xs denote the substitution of four lysine residues (numbers 186, 189, 192, and 195) with glutamic acid residues. (B) Binding of the GST-GBR mutants shown in A to [3H]phosphatidylcholine-labeled vesicles of the indicated compositions. A GST fusion of the β spectrin pleckstrin homology domain (GST-SpecPH) was used as a positive control in the assay.

Image published in: Rohatgi R et al. (2000)

© 2000 The Rockefeller University Press. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license

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