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Role of a tyrosine phosphorylation of SMG-9 in binding of SMG-9 to IQGAP and the NMD complex.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Takeda S,Fujimoto A,Yamauchi E,Hiyoshi M,Kido H,Watanabe T,Kaibuchi K,Ohta T,Konishi H

doi

10.1016/j.bbrc.2011.05.099

subject

Has Abstract

pub_date

2011-06-24 00:00:00

pages

29-33

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00873-4

journal_volume

410

pub_type

杂志文章

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