Jun, 2011
Role of a tyrosine phosphorylation of SMG-9 in binding of SMG-9 to IQGAP and the NMD complex
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- Volume
- 410
- Number
- 1
- First page
- 29
- Last page
- 33
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/j.bbrc.2011.05.099
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
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. (C) 2011 Elsevier Inc. All rights reserved.
- Link information
- ID information
-
- DOI : 10.1016/j.bbrc.2011.05.099
- ISSN : 0006-291X
- Pubmed ID : 21640080
- Web of Science ID : WOS:000292435400006