Purich D L, Southwick F S
Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610-0245, USA.
Biochem Biophys Res Commun. 1997 Feb 24;231(3):686-91. doi: 10.1006/bbrc.1997.6158.
Actin-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).
基于肌动蛋白的运动涉及一系列结合相互作用，旨在将肌动蛋白调节蛋白组装成功能性运动单位。李斯特菌ActA表面蛋白包含一系列几乎相同的EFPPPPTDE型寡聚脯氨酸序列，用于结合血管舒张刺激磷蛋白（VASP）。后者是一种四聚体蛋白，具有许多用于肌动蛋白单体结合蛋白的GPP-PPP对接位点，肌动蛋白单体结合蛋白是一种促进肌动蛋白丝组装的15 kDa调节蛋白。对已知肌动蛋白调节蛋白的分析导致鉴定出不同的基于肌动蛋白的运动同源序列ABM-1；(D/E)FPPPPX(D/E)；和ABM-2，XPPPPP（其中X表示G、A、L和S）。
