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. 2001 Jun 25;153(7):1427–1440. doi: 10.1083/jcb.153.7.1427

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© 2001 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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Paxillin localizes in clusters near the leading edge of the lamellipodium and turns over as new adhesions form. (a) The intensity of paxillin adhesions at the base of new protrusions diminished (thin arrows) and eventually disappeared as adhesions formed in newly protruded region of the lamellipodium (compare t = 600 and t = 0, thick arrows). (b) Plots of the relative intensity of paxillin (from panel a) in the original adhesions (1–3, indicated with thin arrows) and the newly forming adhesions (1′ and 2′) are shown. CHO K1 cells expressing paxillin-GFP were plated on 2 μg/ml Fn. The cells were then fixed and viewed in epifluorescence (c) or by total internal reflection microscopy (d). Note that the paxillin clusters were visible by total internal reflection microscopy, demonstrating their proximity to the substrate. Video 5 available at http://www.jcb.org/cgi/content/full/153/7/1427/DC1. Bars, 10 μm.