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

Saori Takeda, Ai Fujimoto, Emiko Yamauchi, Mineyoshi Hiyoshi, Hiroshi Kido, Takashi Watanabe, Kozo Kaibuchi, Takeshi Ohta, Hiroaki Konishi

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)29-33
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume410
Issue number1
DOIs
Publication statusPublished - 24-06-2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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