http://purl.uniprot.org/citations/22228767 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22228767 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22228767 | http://www.w3.org/2000/01/rdf-schema#comment | "The structural integrity of mitochondrial cristae is crucial for mitochondrial functions; however, the molecular events controlling the structural integrity and biogenesis of mitochondrial cristae remain to be fully elucidated. Here, we report the functional characterization of a novel mitochondrial protein named CHCM1 (coiled coil helix cristae morphology 1)/CHCHD6. CHCM1/CHCHD6 harbors a coiled coil helix-coiled coil helix domain at its C-terminal end and predominantly localizes to mitochondrial inner membrane. CHCM1/CHCHD6 knockdown causes severe defects in mitochondrial cristae morphology. The mitochondrial cristae in CHCM1/CHCHD6-deficient cells become hollow with loss of structural definitions and reduction in electron-dense matrix. CHCM1/CHCHD6 depletion also leads to reductions in cell growth, ATP production, and oxygen consumption. CHCM1/CHCHD6 through its C-terminal end strongly and directly interacts with the mitochondrial inner membrane protein mitofilin, which is known to also control mitochondrial cristae morphology. CHCM1/CHCHD6 also interacts with other mitofilin-associated proteins, including DISC1 and CHCHD3. Knockdown of CHCM1/CHCHD6 reduces mitofilin protein levels; conversely, mitofilin knockdown leads to reduction in CHCM1 levels, suggesting coordinate regulation between these proteins. Our results further indicate that genotoxic anticancer drugs that induce DNA damage down-regulate CHCM1/CHCHD6 expression in multiple human cancer cells, whereas mitochondrial respiratory chain inhibitors do not affect CHCM1/CHCHD6 levels. CHCM1/CHCHD6 knockdown in human cancer cells enhances chemosensitivity to genotoxic anticancer drugs, whereas its overexpression increases resistance. Collectively, our results indicate that CHCM1/CHCHD6 is linked to regulation of mitochondrial cristae morphology, cell growth, ATP production, and oxygen consumption and highlight its potential as a possible target for cancer therapeutics."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.277103"xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.277103"xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "An J."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "An J."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Huang Y."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Huang Y."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Shi J."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Shi J."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "He Q."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "He Q."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Lui K."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Lui K."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Sheikh M.S."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/author | "Sheikh M.S."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/pages | "7411-7426"xsd:string |
http://purl.uniprot.org/citations/22228767 | http://purl.uniprot.org/core/pages | "7411-7426"xsd:string |