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

doi:10.1016/j.bbrc.2011.05.099

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 journal › Article › peer-review

6 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 language	English
Pages (from-to)	29-33
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	410
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2011.05.099
Publication status	Published - 24-06-2011
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2011.05.099

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title = "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.",

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

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doi = "10.1016/j.bbrc.2011.05.099",

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AU - Takeda, Saori

AU - Fujimoto, Ai

AU - Yamauchi, Emiko

AU - Hiyoshi, Mineyoshi

AU - Kido, Hiroshi

AU - Watanabe, Takashi

AU - Kaibuchi, Kozo

AU - Ohta, Takeshi

AU - Konishi, Hiroaki

PY - 2011/6/24

Y1 - 2011/6/24

N2 - 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.

AB - 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.

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

Abstract

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