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pubmed-article:9070872pubmed:abstractTextActin-based motility involves a cascade of binding interactions designed to assemble actin regulatory proteins into functional locomotory units. Listeria ActA surface protein contains a series of nearly identical EFPPPPTDE-type oligoproline sequences for binding vasodilator-stimulated phosphoprotein (VASP). The latter is a tetrameric protein with numerous GPP-PPP docking sites for profilin, a 15 kDa regulatory protein that promotes actin filament assembly. Analysis of known actin regulatory proteins led to the identification of distinct Actin-Based Motility homology sequences ABM-1; (D/E)FPPPPX(D/E); and ABM-2, XPPPPP (where X denotes G, A, L, and S).lld:pubmed
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pubmed-article:9070872pubmed:articleTitleABM-1 and ABM-2 homology sequences: consensus docking sites for actin-based motility defined by oligoproline regions in Listeria ActA surface protein and human VASP.lld:pubmed
pubmed-article:9070872pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610-0245, USA.lld:pubmed
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