کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1930477 | 1050516 | 2011 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: 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](/preview/png/1930477.png)
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.
► IQGAP protein 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.
► Tyrosine phosphorylation of SMG-9 may play a role in the formation of the NMD complex.
Journal: Biochemical and Biophysical Research Communications - Volume 410, Issue 1, 24 June 2011, Pages 29–33