DeFea Kathryn A
Division of Biomedical Sciences and Cell, Molecular, and Developmental Biology Program, University of California, Riverside, California 92521, USA.
Annu Rev Physiol. 2007;69:535-60. doi: 10.1146/annurev.physiol.69.022405.154804.
Beta-arrestins have recently emerged as key regulators of directed cell migration or chemotaxis. Given their traditional role as mediators of receptor desensitization, one theory is that beta-arrestins contribute to cell polarity during chemotaxis by quenching the signal at the trailing edge of the cell. A second theory is that they scaffold signaling molecules involved in cytoskeletal reorganization to promote localized actin assembly events leading to the formation of a leading edge. This review addresses both models. It discusses studies demonstrating the involvement of beta-arrestins in chemotaxis both in vivo and in vitro as well as recent evidence that beta-arrestins directly bind and regulate proteins involved in actin reorganization.
β-抑制蛋白最近已成为定向细胞迁移或趋化作用的关键调节因子。鉴于其作为受体脱敏介质的传统作用,一种理论认为,β-抑制蛋白通过消除细胞后缘的信号来促进趋化作用期间的细胞极性。另一种理论是,它们作为参与细胞骨架重组的信号分子支架,以促进局部肌动蛋白组装事件,从而导致前缘的形成。本综述探讨了这两种模型。它讨论了证明β-抑制蛋白在体内和体外趋化作用中发挥作用的研究,以及β-抑制蛋白直接结合并调节参与肌动蛋白重组的蛋白质的最新证据。