WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac
WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac
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DOI：
10.1016/s0006-291x(02)00218-8
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发表时间：
2002-04-26
影响因子：
3.1
通讯作者：
Takenawa, T
中科院分区：
文献类型：
--
作者：
Miki, H;Takenawa, T
我们先前报道了IRSp 53结合Rac和WAVE 2，诱导Rac/IRSp 53/WAVE 2复合物的形成，这对于膜皱褶是重要的。然而，最近的报告指出，IRSp 53和Cdc 42之间的特定相互作用，而不是Rac。这使我们重新检查IRSp 53与Rac的结合。免疫沉淀分析和pull-down分析表明，全长IRSp 53结合Rac的效率远低于N端片段，这可能是由分子内相互作用引起的。很有趣。分子内相互作用被WAVE 2的结合中断，并且在WAVE 2存在下全长IRSp 53与Rac缔合。我们还报告说，IRSp 53诱导N1 E-115细胞的扩散和轴突形成，这大概反映了与Rac的功能合作。(C)2002年爱思唯尔科学（美国）。All rights reserved.
We previously reported that IRSp53 binds both Rac and WAVE2, inducing formation of Rac/IRSp53/WAVE2 complex that is important for membrane ruffling. However, recent reports noted a specific interaction between IRSp53 and Cdc42 but not Rac. which led us to re-examine the binding of IRSp53 to Rac. Immunoprecipitation analysis and pull-down assay reveal that full-length IRSp53 binds Rac much less efficiently than the N-terminal fragment, which may be caused by intramolecular interaction. Interestingly. the intramolecular interaction is interrupted by the binding of WAVE2 and full-length IRSp53 associates with Rac in the presence of WAVE2. We also report that IRSp53 induces spreading and neurite formation of N1E-115 cells, which presumably reflect functional cooperation with Rac. (C) 2002 Elsevier Science (USA). All rights reserved.