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

研究成果: Article査読

5 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)29-33
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
410
1
DOI
出版ステータスPublished - 24-06-2011
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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