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Review article

CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway

Mio Horii, Hideki Shibata, Ryota Kobayashi, Keiichi Katoh, Chiharu Yorikawa, Jiro Yasuda, Masatoshi Maki
Biochemical Journal Oct 27, 2006, 400 (1) 23-32; DOI: 10.1042/BJ20060897
Mio Horii
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Hideki Shibata
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Ryota Kobayashi
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Keiichi Katoh
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Chiharu Yorikawa
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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Jiro Yasuda
Fifth Biology Section for Microbiology, Department of First Forensic Science, National Research Institute of Police Science, Kashiwanoha 6-3-1, Kashiwa 277-0882, Japan
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Masatoshi Maki
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan
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  • For correspondence: mmaki@agr.nagoya-u.ac.jp
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Abstract

All CHMPs (charged multivesicular body proteins) reported to date have common features: they all contain approx. 200 amino acid residues, have coiled-coil regions and have a biased distribution of charged residues (basic N-terminal and acidic C-terminal halves). Yeast orthologues of CHMPs, including an ESCRT-III component Snf7, are required for the sorting of cargo proteins to intraluminal vesicles of multivesicular bodies. We have characterized a novel human ESCRT-III-related protein, designated CHMP7, which consists of 453 amino acid residues. CHMP7 contains an SNF7 domain and a distantly SNF7-related domain in its C-terminal half and N-terminal half respectively. Among the ten CHMP proteins classified previously in six subfamilies (CHMP1–CHMP6), the C-terminal SNF7 domain of CHMP7 is most similar to the SNF7 domain of CHMP6, which associates with CHMP4 proteins and EAP20, a component of ESCRT-II. Pull-down assays using lysates of HEK-293T (human embryonic kidney) cells that overexpressed Strep-tagged CHMP7 and GFP (green fluorescent protein)-fused CHMP4b (also named Shax1) revealed a positive interaction between the C-terminal half of CHMP7 and CHMP4b. However, interaction was not observed between CHMP7 and EAP20. Confocal fluorescence microscopic analyses revealed that FLAG–CHMP7 is distributed in HeLa cells diffusely throughout the cytoplasm, but with some accumulation, especially in the perinuclear area. The distribution of FLAG–CHMP7 was altered to a cytoplasmic punctate pattern by overexpression of either CHMP4b–GFP or GFP–Vps4BE235Q, a dominant-negative mutant of the AAA (ATPase associated with various cellular activities) Vps4B, and partially co-localized with them. Ubiquitinated proteins and endocytosed EGF accumulated in GFP–CHMP7-expressing cells. A dominant-negative effect of overexpressed GFP–CHMP7 was also observed in the release of virus-like particles from HEK-293T cells that transiently expressed the MLV (murine leukaemia virus) Gag protein. These results suggest that CHMP7, a novel CHMP4-associated ESCRT-III-related protein, functions in the endosomal sorting pathway.

  • changed multivesicular body protein (CHMP)
  • endosomal sorting complex required for transport (ESCRT)
  • multivesicular body
  • retrovirus
  • SNF7

Abbreviations: AAA, ATPase associated with various cellular activities; AD, transcription-activation domain; Alix, ALG-2-interacting protein X; BD, DNA-binding domain; CaM, calmodulin; CC, coiled coil; CDD, conserved domain database; CHMP, charged multivesicular body protein; CHMP7NH, N-terminal half of CHMP7; CHMP7CH, C-terminal half of CHMP7; DMEM, Dulbecco's modified Eagle's medium; EEA1, early endosome antigen 1; EGF, epidermal growth factor; ESCRT, endosomal sorting complex required for transport; FBS, foetal bovine serum; GFP, green fluorescent protein; GST, glutathione S-transferase; HEK-293, human embryonic kidney; HRP, horseradish peroxidase; Lamp1, lysosome-associated membrane protein 1; mAb, monoclonal antibody; MLV, murine leukaemia virus; mRFP, monomeric red fluorescent protein; MVB, multivesicular body; Rh, tetramethylrhodamine; VLP, virus-like particle

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November 2006

Volume: 400 Issue: 1

Biochemical Journal: 400 (1)
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CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway
Mio Horii, Hideki Shibata, Ryota Kobayashi, Keiichi Katoh, Chiharu Yorikawa, Jiro Yasuda, Masatoshi Maki
Biochemical Journal Nov 2006, 400 (1) 23-32; DOI: 10.1042/BJ20060897
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CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway
Mio Horii, Hideki Shibata, Ryota Kobayashi, Keiichi Katoh, Chiharu Yorikawa, Jiro Yasuda, Masatoshi Maki
Biochemical Journal Nov 2006, 400 (1) 23-32; DOI: 10.1042/BJ20060897

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Keywords

changed multivesicular body protein (CHMP)
endosomal sorting complex required for transport (ESCRT)
multivesicular body
retrovirus
Snf7

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