SDH5, a Gene Required for Flavination of Succinate Dehydrogenase, Is Mutated in Paraganglioma
Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we in...
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| Published in | Science (American Association for the Advancement of Science) Vol. 325; no. 5944; pp. 1139 - 1142 |
|---|---|
| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Washington, DC
American Association for the Advancement of Science
28.08.2009
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene. |
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| AbstractList | Mitochondria produce the energy that cells need to survive, function, and divide. A growing list of human disorders has been traced to defects in mitochondrial function. About 300 mammalian mitochondrial proteins are functionally uncharacterized, and
Hao
et al.
(p.
1139
, published online 23 July) reasoned that the most highly conserved proteins within this group might provide insights into human disease. A combination of bioinformatics, yeast genetics, biochemistry, and human genetics was used to show that a previously uncharacterized mitochondrial protein (Sdh5) is required for the activity of respiratory complex II. Inactivating mutations in the human gene encoding
SDH5
were found in individuals with hereditary paraganglioma, a rare neuroendocrine tumor. Thus, analysis of a mitochondrial protein in yeast has revealed a human tumor susceptibility gene.
Analysis of a yeast mitochondrial protein reveals a human tumor susceptibility gene.
Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human
SDH5
gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene. Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene. Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene.Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene. Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene. |
| Author | Devilee, Peter Khalimonchuk, Oleh Cremers, Cor W.R.J Bentz, Brandon G Hao, Huai-Xiang Schiffman, Joshua D Gygi, Steven P Rutter, Jared Kunst, Henricus Schraders, Margit Bayley, Jean-Pierre Winge, Dennis R Kremer, Hannie Dephoure, Noah |
| AuthorAffiliation | 8 Department of Human Genetics, Leiden University Medical Centre, Leiden 2333 ZA, Netherlands 1 Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 2 Department of Internal Medicine, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 7 Department of Cell Biology, Harvard University Medical School, 240 Longwood Avenue, Boston, MA 02115, USA 4 Department of Surgery, Division of Otolaryngology–Head and Neck Surgery, University of Utah School of Medicine, Salt Lake City, UT 84112, USA 9 Department of Pathology, Leiden University Medical Centre, Leiden 2333 ZA, Netherlands 3 Department of Oncological Sciences and Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT, 84112, USA 5 Department of Otorhinolaryngology, Donders Centre for Brain, Cognition and Behaviour, Radboud University Nijmegen Medical Centre, Nijmegen 6500 HB, Netherlands 6 Centre for Molecular Life Sciences, Radboud University Nijmegen Medi |
| AuthorAffiliation_xml | – name: 3 Department of Oncological Sciences and Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT, 84112, USA – name: 5 Department of Otorhinolaryngology, Donders Centre for Brain, Cognition and Behaviour, Radboud University Nijmegen Medical Centre, Nijmegen 6500 HB, Netherlands – name: 6 Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen 6500 HB, Netherlands – name: 2 Department of Internal Medicine, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 8 Department of Human Genetics, Leiden University Medical Centre, Leiden 2333 ZA, Netherlands – name: 1 Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 4 Department of Surgery, Division of Otolaryngology–Head and Neck Surgery, University of Utah School of Medicine, Salt Lake City, UT 84112, USA – name: 9 Department of Pathology, Leiden University Medical Centre, Leiden 2333 ZA, Netherlands – name: 7 Department of Cell Biology, Harvard University Medical School, 240 Longwood Avenue, Boston, MA 02115, USA |
| Author_xml | – sequence: 1 fullname: Hao, Huai-Xiang – sequence: 2 fullname: Khalimonchuk, Oleh – sequence: 3 fullname: Schraders, Margit – sequence: 4 fullname: Dephoure, Noah – sequence: 5 fullname: Bayley, Jean-Pierre – sequence: 6 fullname: Kunst, Henricus – sequence: 7 fullname: Devilee, Peter – sequence: 8 fullname: Cremers, Cor W.R.J – sequence: 9 fullname: Schiffman, Joshua D – sequence: 10 fullname: Bentz, Brandon G – sequence: 11 fullname: Gygi, Steven P – sequence: 12 fullname: Winge, Dennis R – sequence: 13 fullname: Kremer, Hannie – sequence: 14 fullname: Rutter, Jared |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21904869$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/19628817$$D View this record in MEDLINE/PubMed |
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| Snippet | Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human... Mitochondria produce the energy that cells need to survive, function, and divide. A growing list of human disorders has been traced to defects in mitochondrial... |
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| SubjectTerms | Adenine Amino Acid Sequence Antibodies Biological and medical sciences Cell Line Cell Line, Tumor chromosomes Dehydrogenases electron transport chain Female flavin-adenine dinucleotide Flavin-Adenine Dinucleotide - metabolism Flavoproteins - metabolism Fluorescence Genes Genetic mutation germ cells Germ-Line Mutation Haplotypes human diseases Humans Inheritance Patterns loss-of-function mutation Male Medical sciences Mitochondria Mitochondria - metabolism Mitochondrial Proteins - chemistry Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Molecular Sequence Data Nervous system diseases Neurology Oxygen Consumption Paraganglioma - genetics Pedigree Plasmids protein subunits Protein Subunits - metabolism proteins Proteomics Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism succinate dehydrogenase (quinone) Succinate Dehydrogenase - metabolism tricarboxylic acid cycle Tumors Tumors of the nervous system. Phacomatoses Yeasts |
| Title | SDH5, a Gene Required for Flavination of Succinate Dehydrogenase, Is Mutated in Paraganglioma |
| URI | https://www.jstor.org/stable/20544416 https://www.ncbi.nlm.nih.gov/pubmed/19628817 https://www.proquest.com/docview/20786646 https://www.proquest.com/docview/46380223 https://www.proquest.com/docview/67614126 https://pubmed.ncbi.nlm.nih.gov/PMC3881419 |
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