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. 2008 Jul 14;182(1):157–169. doi: 10.1083/jcb.200801042

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© 2008 Oikawa et al.

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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — The plasma membrane at the podosomes in NIH-src cells is enriched with PtdIns(3,4)P2. (A) Localization of phosphoinositide-binding domains in NIH-src cells. PtdIns(3)P, PtdIns(4)P, PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3 were localized by the FYVE domain of Hrs and the PH domains of Fapp1, PLCδ1, Tapp1, Grp1, and Akt, respectively. In the figure, 2× indicates two domains linked in tandem. The binding specificity of the constructs for each domain has been described previously (Furutani et al., 2006). The cells were stained with rhodamine-phalloidin (red) to visualize F-actin with anti-HA or anti-myc antibody (green). Bars, 20 μm. (B) Quantification of podosomes in NIH-src cells expressing lipid-binding domains (regardless of its expression amount). Error bars represent the standard deviations of three independent measurements. *, P < 0.04; **, P < 0.02 by Student's t test compared with each mutant (Tapp1PH and AktPH). A minimum of 50 cells were counted for each determination.