Mutations in FBXL4, Encoding a Mitochondrial Protein, Cause Early-Onset Mitochondrial Encephalomyopathy
Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons...
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| Published in | American journal of human genetics Vol. 93; no. 3; pp. 482 - 495 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
05.09.2013
Cell Press Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0002-9297 1537-6605 1537-6605 |
| DOI | 10.1016/j.ajhg.2013.07.016 |
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| Abstract | Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy. |
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| AbstractList | Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy. Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy. [PUBLICATION ABSTRACT] Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy. Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy.Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings. All subjects manifested early-onset lactic acidemia, hypotonia, and developmental delay caused by severe encephalomyopathy consistently associated with progressive cerebral atrophy and variable involvement of the white matter, deep gray nuclei, and brainstem structures. A wide range of other multisystem features were variably seen, including dysmorphism, skeletal abnormalities, poor growth, gastrointestinal dysmotility, renal tubular acidosis, seizures, and episodic metabolic failure. Mitochondrial respiratory chain deficiency was present in muscle or fibroblasts of all tested individuals, together with markedly reduced oxygen consumption rate and hyperfragmentation of the mitochondrial network in cultured cells. In muscle and fibroblasts from several subjects, substantially decreased mtDNA content was observed. FBXL4 is a member of the F-box family of proteins, some of which are involved in phosphorylation-dependent ubiquitination and/or G protein receptor coupling. We also demonstrate that FBXL4 is targeted to mitochondria and localizes in the intermembrane space, where it participates in an approximately 400 kDa protein complex. These data strongly support a role for FBXL4 in controlling bioenergetic homeostasis and mtDNA maintenance. FBXL4 mutations are a recurrent cause of mitochondrial encephalomyopathy onset in early infancy. |
| Author | Konstantopoulou, Vassiliki Srinivasan, Satish Furlan, Francesca Shamseldin, Hanan E. Mayr, Johannes A. Ghezzi, Daniele Meitinger, Thomas Al-Jishi, Emtethal Kremer, Laura S. Strom, Tim M. Biagosch, Caroline A. Raab, Christopher P. Zeviani, Massimo Sondheimer, Neal Ostrovsky, Julian Wong, Lee-Jun Bean, Charles Johnson, Mark A. Reyes, Aurelio Lamperti, Costanza Salih, Mustafa A. Freisinger, Peter Alkuraya, Fowzan S. Polyak, Erzsebet Wieland, Thomas Vidoni, Sara Gai, Xiaowu Consugar, Mark Parini, Rossella Sperl, Wolfgang Tsukikawa, Mai Huemer, Martina Gorza, Matteo Robinson, Alan J. Sheldon, Claire A. Falk, Marni J. Haack, Tobias B. Prokisch, Holger Pierce, Eric A. Place, Emily |
| AuthorAffiliation | 3 MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK 5 Institute of Human Genetics, Helmholtz Zentrum Munich, 81675 Munich, Germany 15 Department of Paediatrics, Paracelsus Medical University Salzburg, 5020 Salzburg, Austria 16 Department of Pediatrics, Medical University of Vienna, 1090 Vienna, Austria 11 Department of Pediatrics, King Khalid University Hospital and College of Medicine, King Saud University, 11461 Riyadh, Saudi Arabia 12 Salmaniya Medical Complex, Arabian Gulf University, P.O. Box 26671, Bahrain 14 Unit of Metabolic Disorders, Department of Pediatrics, Foundation MBBM/San Gerardo University Hospital, 20900 Monza, Italy 10 Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA 17 Department of Pediatrics, LKH Bregenz, 6900 Bregenz, Austria 2 Department of Molecular Neurogenetics, Institute of Neurology Besta, 23888 Milan, Italy 8 Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, PA 191 |
| AuthorAffiliation_xml | – name: 12 Salmaniya Medical Complex, Arabian Gulf University, P.O. Box 26671, Bahrain – name: 20 Department of Anatomy and Cell Biology, College of Medicine, Alfaisal University, 11533 Riyadh, Saudi Arabia – name: 19 Department of Pediatrics, Klinikum Reutlingen, 72764 Reutlingen, Germany – name: 8 Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, PA 19104, USA – name: 11 Department of Pediatrics, King Khalid University Hospital and College of Medicine, King Saud University, 11461 Riyadh, Saudi Arabia – name: 1 Department of Molecular Pharmacology and Therapeutics, Loyola University Stritch School of Medicine, Maywood, IL 60153, USA – name: 3 MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK – name: 5 Institute of Human Genetics, Helmholtz Zentrum Munich, 81675 Munich, Germany – name: 17 Department of Pediatrics, LKH Bregenz, 6900 Bregenz, Austria – name: 15 Department of Paediatrics, Paracelsus Medical University Salzburg, 5020 Salzburg, Austria – name: 7 Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – name: 2 Department of Molecular Neurogenetics, Institute of Neurology Besta, 23888 Milan, Italy – name: 18 Berman-Gund Laboratory for the Study of Retinal Degenerations, Department of Ophthalmology, MEEI, Harvard Medical School, Boston, MA 02114, USA – name: 4 Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – name: 10 Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA – name: 14 Unit of Metabolic Disorders, Department of Pediatrics, Foundation MBBM/San Gerardo University Hospital, 20900 Monza, Italy – name: 9 Ocular Genomics Institute, Massachusetts Eye and Ear Infirmary (MEEI), Harvard Medical School, Boston, MA 02114, USA – name: 13 Department of Pediatrics, Nemours/AI DuPont Hospital for Children, Thomas Jefferson University, Wilmington, DE 19803, USA – name: 16 Department of Pediatrics, Medical University of Vienna, 1090 Vienna, Austria – name: 6 Department of Genetics, King Faisal Specialist Hospital and Research Center, 11211 Riyadh, Saudi Arabia |
| Author_xml | – sequence: 1 givenname: Xiaowu surname: Gai fullname: Gai, Xiaowu organization: Department of Molecular Pharmacology and Therapeutics, Loyola University Stritch School of Medicine, Maywood, IL 60153, USA – sequence: 2 givenname: Daniele surname: Ghezzi fullname: Ghezzi, Daniele organization: Department of Molecular Neurogenetics, Institute of Neurology Besta, 23888 Milan, Italy – sequence: 3 givenname: Mark A. surname: Johnson fullname: Johnson, Mark A. organization: MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK – sequence: 4 givenname: Caroline A. surname: Biagosch fullname: Biagosch, Caroline A. organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 5 givenname: Hanan E. surname: Shamseldin fullname: Shamseldin, Hanan E. organization: Department of Genetics, King Faisal Specialist Hospital and Research Center, 11211 Riyadh, Saudi Arabia – sequence: 6 givenname: Tobias B. surname: Haack fullname: Haack, Tobias B. organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 7 givenname: Aurelio surname: Reyes fullname: Reyes, Aurelio organization: MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK – sequence: 8 givenname: Mai surname: Tsukikawa fullname: Tsukikawa, Mai organization: Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – sequence: 9 givenname: Claire A. surname: Sheldon fullname: Sheldon, Claire A. organization: Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – sequence: 10 givenname: Satish surname: Srinivasan fullname: Srinivasan, Satish organization: Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, PA 19104, USA – sequence: 11 givenname: Matteo surname: Gorza fullname: Gorza, Matteo organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 12 givenname: Laura S. surname: Kremer fullname: Kremer, Laura S. organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 13 givenname: Thomas surname: Wieland fullname: Wieland, Thomas organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 14 givenname: Tim M. surname: Strom fullname: Strom, Tim M. organization: Institute of Human Genetics, Technical University Munich, 81675 Munich, Germany – sequence: 15 givenname: Erzsebet surname: Polyak fullname: Polyak, Erzsebet organization: Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – sequence: 16 givenname: Emily surname: Place fullname: Place, Emily organization: Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – sequence: 17 givenname: Mark surname: Consugar fullname: Consugar, Mark organization: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA – sequence: 18 givenname: Julian surname: Ostrovsky fullname: Ostrovsky, Julian organization: Department of Animal Biology, University of Pennsylvania School of Veterinary Medicine, Philadelphia, PA 19104, USA – sequence: 19 givenname: Sara surname: Vidoni fullname: Vidoni, Sara organization: MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK – sequence: 20 givenname: Alan J. surname: Robinson fullname: Robinson, Alan J. organization: MRC Mitochondrial Biology Unit, Cambridge CB2 0XY, UK – sequence: 21 givenname: Lee-Jun surname: Wong fullname: Wong, Lee-Jun organization: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA – sequence: 22 givenname: Neal surname: Sondheimer fullname: Sondheimer, Neal organization: Divisions of Human Genetics and Metabolic Disease, Department of Pediatrics, Children’s Hospital of Philadelphia and University of Pennsylvania Perleman School of Medicine, Philadelphia, PA 19104, USA – sequence: 23 givenname: Mustafa A. surname: Salih fullname: Salih, Mustafa A. organization: Department of Pediatrics, King Khalid University Hospital and College of Medicine, King Saud University, 11461 Riyadh, Saudi Arabia – sequence: 24 givenname: Emtethal surname: Al-Jishi fullname: Al-Jishi, Emtethal organization: Salmaniya Medical Complex, Arabian Gulf University, P.O. 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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23993194$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | 2013 The American Society of Human Genetics Copyright © 2013 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved. Copyright Cell Press Sep 5, 2013 2013 The American Society of Human Genetics. Published by Elsevier Ltd. All right reserved. 2013 The American Society of Human Genetics |
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| SubjectTerms | Age of Onset Cell culture Child Child, Preschool Chromosomes, Human, Pair 6 - genetics DNA, Complementary - genetics F-Box Proteins - chemistry F-Box Proteins - genetics Female Fibroblasts - metabolism Fibroblasts - pathology Genes, Recessive - genetics Genetic Predisposition to Disease HEK293 Cells Homeostasis Humans Infant Infant, Newborn Male Mitochondria - metabolism Mitochondrial DNA Mitochondrial Encephalomyopathies - epidemiology Mitochondrial Encephalomyopathies - genetics Mitochondrial Proteins - genetics Muscle, Skeletal - pathology Mutant Proteins - metabolism Mutation Mutation - genetics Oxidative Phosphorylation Pedigree Phosphorylation Protein Transport Proteins Subcellular Fractions - metabolism Syndrome Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics |
| Title | Mutations in FBXL4, Encoding a Mitochondrial Protein, Cause Early-Onset Mitochondrial Encephalomyopathy |
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