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http://purl.uniprot.org/citations/16856878http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16856878http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16856878http://www.w3.org/2000/01/rdf-schema#comment"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-Vps4B(E235Q), 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."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.org/dc/terms/identifier"doi:10.1042/bj20060897"xsd:string
http://purl.uniprot.org/citations/16856878http://purl.org/dc/terms/identifier"doi:10.1042/bj20060897"xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Yasuda J."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Yasuda J."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Katoh K."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Katoh K."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Horii M."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Horii M."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Yorikawa C."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/author"Yorikawa C."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/pages"23-32"xsd:string
http://purl.uniprot.org/citations/16856878http://purl.uniprot.org/core/pages"23-32"xsd:string
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