Cullin-3/KCTD10 complex is essential for K27-polyubiquitination of EIF3D in human hepatocellular carcinoma HepG2 cells

Masashi Maekawa, Hiromi Hiyoshi, Jun Nakayama, K. Kido, Tatsuya Sawasaki, Kentaro Semba, Eiji Kubota, Takashi Joh, Shigeki Higashiyama

研究成果: Article

抄録

Eukaryotic translation initiation factor 3 subunit D (EIF3D) binds to the 5′-cap of specific mRNAs, initiating their translation into polypeptides. From a pathological standpoint, EIF3D has been observed to be essential for cell growth in various cancer types, and cancer patients with high EIF3D mRNA levels exhibit poor prognosis, indicating involvement of EIF3D in oncogenesis. In this study, we found, by mass spectrometry, that Cullin-3 (CUL3)/KCTD10 ubiquitin (Ub) ligase forms a complex with EIF3D. We also demonstrated that EIF3D is K27-polyubiquitinated at the lysine 153 and 275 residues in a KCTD10-dependent manner in human hepatocellular carcinoma HepG2 cells. Similar to other cancers, high expression of EIF3D significantly correlated with poor prognosis in hepatocellular carcinoma patients, and depletion of EIF3D drastically suppressed HepG2 cell proliferation. These results indicate that EIF3D is a novel substrate of CUL3/KCTD10 Ub ligase and suggest involvement of K27-polyubiquitinated EIF3D in the development of hepatocellular carcinoma.

元の言語English
ジャーナルBiochemical and Biophysical Research Communications
DOI
出版物ステータスPublished - 2019 1 1

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Prokaryotic Initiation Factor-3
Eukaryotic Initiation Factor-3
Cullin Proteins
Eukaryotic Initiation Factors
Hep G2 Cells
Hepatocellular Carcinoma
Ligases
Ubiquitin
Neoplasms
Messenger RNA
Cell proliferation
Cell growth
Lysine
Mass spectrometry

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Cullin-3/KCTD10 complex is essential for K27-polyubiquitination of EIF3D in human hepatocellular carcinoma HepG2 cells. / Maekawa, Masashi; Hiyoshi, Hiromi; Nakayama, Jun; Kido, K.; Sawasaki, Tatsuya; Semba, Kentaro; Kubota, Eiji; Joh, Takashi; Higashiyama, Shigeki.

:: Biochemical and Biophysical Research Communications, 01.01.2019.

研究成果: Article

Maekawa, Masashi ; Hiyoshi, Hiromi ; Nakayama, Jun ; Kido, K. ; Sawasaki, Tatsuya ; Semba, Kentaro ; Kubota, Eiji ; Joh, Takashi ; Higashiyama, Shigeki. / Cullin-3/KCTD10 complex is essential for K27-polyubiquitination of EIF3D in human hepatocellular carcinoma HepG2 cells. :: Biochemical and Biophysical Research Communications. 2019.
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abstract = "Eukaryotic translation initiation factor 3 subunit D (EIF3D) binds to the 5′-cap of specific mRNAs, initiating their translation into polypeptides. From a pathological standpoint, EIF3D has been observed to be essential for cell growth in various cancer types, and cancer patients with high EIF3D mRNA levels exhibit poor prognosis, indicating involvement of EIF3D in oncogenesis. In this study, we found, by mass spectrometry, that Cullin-3 (CUL3)/KCTD10 ubiquitin (Ub) ligase forms a complex with EIF3D. We also demonstrated that EIF3D is K27-polyubiquitinated at the lysine 153 and 275 residues in a KCTD10-dependent manner in human hepatocellular carcinoma HepG2 cells. Similar to other cancers, high expression of EIF3D significantly correlated with poor prognosis in hepatocellular carcinoma patients, and depletion of EIF3D drastically suppressed HepG2 cell proliferation. These results indicate that EIF3D is a novel substrate of CUL3/KCTD10 Ub ligase and suggest involvement of K27-polyubiquitinated EIF3D in the development of hepatocellular carcinoma.",
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AU - Maekawa, Masashi

AU - Hiyoshi, Hiromi

AU - Nakayama, Jun

AU - Kido, K.

AU - Sawasaki, Tatsuya

AU - Semba, Kentaro

AU - Kubota, Eiji

AU - Joh, Takashi

AU - Higashiyama, Shigeki

PY - 2019/1/1

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AB - Eukaryotic translation initiation factor 3 subunit D (EIF3D) binds to the 5′-cap of specific mRNAs, initiating their translation into polypeptides. From a pathological standpoint, EIF3D has been observed to be essential for cell growth in various cancer types, and cancer patients with high EIF3D mRNA levels exhibit poor prognosis, indicating involvement of EIF3D in oncogenesis. In this study, we found, by mass spectrometry, that Cullin-3 (CUL3)/KCTD10 ubiquitin (Ub) ligase forms a complex with EIF3D. We also demonstrated that EIF3D is K27-polyubiquitinated at the lysine 153 and 275 residues in a KCTD10-dependent manner in human hepatocellular carcinoma HepG2 cells. Similar to other cancers, high expression of EIF3D significantly correlated with poor prognosis in hepatocellular carcinoma patients, and depletion of EIF3D drastically suppressed HepG2 cell proliferation. These results indicate that EIF3D is a novel substrate of CUL3/KCTD10 Ub ligase and suggest involvement of K27-polyubiquitinated EIF3D in the development of hepatocellular carcinoma.

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