Holt M R, Critchley D R, Brindle N P
Department of Biochemistry, University of Leicester, U.K.
Int J Biochem Cell Biol. 1998 Mar;30(3):307-11. doi: 10.1016/s1357-2725(97)00101-5.
Vasodilator-stimulated phosphoprotein (VASP) is associated with focal adhesions and areas of dynamic membrane activity, where it is thought to have an important role in actin filament assembly and cell motility. VASP contains a central proline-rich sequence which recruits the G-actin binding protein profilin. Localization of VASP to the leading edge of a migrating cell can lead to local accumulation of profilin, which in turn can supply actin monomers to growing filament ends. VASP binds to the focal adhesion proteins vinculin and zyxin and this probably directs the phosphoprotein to focal adhesions and the leading edge of stimulated cells. VASP functions as a binding intermediate between profilin and focal adhesion proteins. Intracellular pathogens, including Listeria monocytogenes, have coat proteins which bind VASP. This is one way in which these pathogens use VASP, and other proteins from the host cell, to assemble the actin filaments they require to move around the cytoplasm of infected cells and enter neighbouring cells. Understanding the role of VASP and other proteins in cell and bacterial motility is likely to lead to development of new therapeutic strategies for diseases including atherosclerosis and tumour growth, and for limiting the spread of intracellular pathogens.
血管舒张刺激磷蛋白（VASP）与粘着斑和动态膜活动区域相关，据认为它在肌动蛋白丝组装和细胞运动中起重要作用。VASP含有一个富含脯氨酸的中央序列，该序列可募集G-肌动蛋白结合蛋白丝切蛋白。VASP定位于迁移细胞的前沿可导致丝切蛋白在局部积累，进而可为生长中的丝末端提供肌动蛋白单体。VASP与粘着斑蛋白纽蛋白和斑联蛋白结合，这可能将该磷蛋白导向粘着斑和受刺激细胞的前沿。VASP作为丝切蛋白和粘着斑蛋白之间的结合中间体发挥作用。包括单核细胞增生李斯特菌在内的细胞内病原体具有与VASP结合的外壳蛋白。这是这些病原体利用VASP和宿主细胞的其他蛋白来组装它们在被感染细胞的细胞质中移动并进入相邻细胞所需的肌动蛋白丝的一种方式。了解VASP和其他蛋白在细胞和细菌运动中的作用可能会导致开发针对包括动脉粥样硬化和肿瘤生长在内的疾病以及限制细胞内病原体传播的新治疗策略。
