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. 2000 Sep 18;150(6):1299–1310. doi: 10.1083/jcb.150.6.1299

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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The BR in the NH₂ terminus is required for the ability of PI(4,5)P₂ to activate N-WASP. (A) A 10% SDS–polyacrylamide gel showing purified protein preparations of wild-type GST-N-WASP or a GST-tagged mutant of N-WASP containing an internal deletion of the BR (GST-(ΔB)N-WASP). (B) The maximum rate of polymerization was used to quantitate Arp2/3 activity (1.3 μM actin, 30 nM Arp2/3 complex) in the presence of two different concentrations of GST-N-WASP or GST-(ΔB) N-WASP and the indicated combinations of Cdc42-GTPγS (450 nM) and PI(4,5)P₂-containing vesicles. While the data shown in B is at 1 μM lipid, GST-(ΔB)N-WASP was PI(4,5)P₂-insensitive at higher lipid concentrations as well (up to 5 μM).