Role of a tyrosine phosphorylation of SMG-9 in binding of SMG-9 to IQGAP and the NMD complex
Role of a tyrosine phosphorylation of SMG-9 in binding of SMG-9 to IQGAP and the NMD complex
复制标题
SMG-9 酪氨酸磷酸化在 SMG-9 与 IQGAP 和 NMD 复合物结合中的作用
DOI：
10.1016/j.bbrc.2011.05.099
复制
发表时间：
2011
影响因子：
3.1
通讯作者：
et al
中科院分区：
文献类型：
--
作者：
Takeda S.;et al
SMG-9是NMD复合物的组分，NMD复合物是一种异源四聚体，在复合物中还包括SMG-1和SMG-8。SMG-9最初也被鉴定为酪氨酸磷酸化蛋白，但磷酸化的作用尚不清楚。在这项研究中，我们确定了IQGAP蛋白，肌动蛋白细胞骨架修饰剂作为与SMG-9的结合伴侣，这种结合受SMG-9在Tyr-41的磷酸化调节。SMG-9与IQGAP 1共定位，作为非刺激细胞中肌动蛋白富集过程的一部分，但不在EGF刺激的细胞中。此外，SMG-9与SMG-8结合的能力增加是对EGF刺激的反应。这些结果表明，SMG-9的酪氨酸磷酸化可能在生长因子刺激的细胞中NMD复合物的形成中起作用。
SMG-9 is a component of the NMD complex, a heterotetramer that also includes SMG-1 and SMG-8 in the complex. SMG-9 was also originally identified as a tyrosine-phosphorylated protein but the role of the phosphorylation is not yet known. In this study, we determined that IQGAP protein, an actin cytoskeleton modifier acts as a binding partner with SMG-9 and this binding is regulated by phosphorylation of SMG-9 at Tyr-41. SMG-9 is co-localized with IQGAP1 as a part of the process of actin enrichment in non-stimulated cells, but not in the EGF-stimulated cells. Furthermore, an increase in the ability of SMG-9 to bind to SMG-8 occurs in response to EGF stimulation. These results suggest that tyrosine phosphorylation of SMG-9 may play a role in the formation of the NMD complex in the cells stimulated by the growth factor.