Structure and function of vav
Structure and function of vav
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DOI：
10.1016/s0898-6568(96)00118-0
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发表时间：
1996-12-01
影响因子：
4.8
通讯作者：
Fischer, S
中科院分区：
文献类型：
--
作者：
Romero, F;Fischer, S
原癌基因vav仅在造血来源的细胞中表达，而与其分化谱系无关。然而，最近已经鉴定了广泛表达的vav的同源物（vav 2）。Vav是一种复杂而有趣的分子，它包含许多在参与细胞信号传导的蛋白质中发现的结构特征。Vav具有富含亮氨酸的区域、亮氨酸拉链、钙调蛋白同源结构域、酸性结构域、Dbl-同源结构域、普列克底物蛋白同源结构域、富含半胱氨酸的结构域、两个Src同源3结构域，在氨基SH中具有富含脯氨酸的区域。结构域，最后是Src同源2结构域。这些结构域与蛋白质-蛋白质相互作用有关，强烈提示vav参与信号传导。VAV还通过激活造血细胞上的多种受体而快速和瞬时地酪氨酸磷酸化。此外，vav在几种细胞因子和生长因子的激活后被酪氨酸磷酸化。最近，小鼠vav（-/-）的产生表明vav在T和B细胞的增殖/活化中具有重要作用。本文就vav的研究进展及vav在细胞功能中的作用作一综述。版权所有（C）1996 Elsevier Science Inc.
The proto-oncogene vav is expressed solely in cells of hematopoietic origin regardless of their differentiation lineage. However, recently an homologue of vav, which is widely expressed (vav2) has been identified. Vav is a complicated and interesting molecule that contains a number of structural features found in proteins involved in cell signaling. Vav has a leucine rich region, a leucine zipper, a calponin homology domain, an acidic domain, a Dbl-homology domain, a pleckstrin homology domain, a cysteine-rich domain, two Src homology 3 domains, with a proline-rich region in the amino SH? domain, and finally an Src homology 2 domain. These domains have been implicated in protein-protein interactions and strongly suggest that vav is involved in signaling events. vav is also rapidly and transiently tyrosine phosphorylated through the activation of multiple receptors on hematopoietic cells. Furthermore, vav, is tyrosine phosphorylated upon the activation of several cytokines and growths factors. Recently, the generation of mice vav(-/-) showed that vav, has an essential role in proliferation/activation of T and B cells. The purpose of this review is to summarize the current knowledge on vav and to evaluate the roles of vav, in cellular functions. Copyright (C) 1996 Elsevier Science Inc.