细胞信号转导文献2.pdfVIP

97 Control of actin assembly and disassembly at filament ends John A Cooper* and Dorothy A Schafer† The most important discovery in the field is that the Arp2/3 proteins affect actin polymerization. One exciting exam- complex nucleates assembly of actin filaments with free barbed ple is the discovery that three actin-binding proteins, plus ends. Arp2/3 also binds the sides of actin filaments to create a actin, are sufficient for Listeria to induce actin polymeriza- branched network. Arp2/3’s nucleation activity is stimulated by tion and motility [1••]. WASP family proteins, some of which mediate signaling from small G-proteins. Listeria movement caused by actin This field has been the subject of a number of reviews in polymerization can be reconstituted in vitro using purified recent years. We reviewed this topic in more depth sever- proteins: Arp2/3 complex, capping protein, actin al years ago [2]. More recent reviews have addressed depolymerizing factor/cofilin, and actin. actin depolymerizing filament length in muscle [3], actin polymerization dynam- factor/cofilin increases the rate at which actin subunits leave ics and signaling [4], how WASP links small G proteins to pointed ends, and capping protein caps barbed ends. Arp2/3 complex [5], how Arp2/3 complex functions [6–8], how ADF/cofilin proteins function [9,10] and how gelsolin Addresses and its relatives function [11]. In this minireview, we focus Department of Cell Biology, Washington University, Box 8