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. 2001 Jun 25;153(7):1403–1414. doi: 10.1083/jcb.153.7.1403

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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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APP and FE65 probably regulate membrane motility as part of a larger macromolecular complex. The schematic depicts the possible components of the macromolecular complex and their putative interactions. FE65 might interact with APP through its COOH-terminal PID and with Mena through its WW domain. Mena modulates actin polymerization, possibly through its interaction with profilin, whereas integrins are indirectly linked to actin through a variety of integrin- and actin-binding proteins, such as α-actinin. Regulation of the various interactions shown could connect environmental cues to actin dynamics at the lamellipodial focal complex.