ATPase-deficient mitochondrial inner membrane protein ATAD3A disturbs mitochondrial dynamics in dominant hereditary spastic paraplegia
De novo mutations in ATAD3A (ATPase family AAA-domain containing protein 3A) were recently found to cause a neurological syndrome with developmental delay, hypotonia, spasticity, optic atrophy, axonal neuropathy, and hypertrophic cardiomyopathy. Using whole-exome sequencing, we identified a dominant...
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| Vydané v: | Human molecular genetics Ročník 26; číslo 8; s. 1432 - 1443 |
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| Hlavní autori: | , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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15.04.2017
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| ISSN: | 1460-2083 |
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| Abstract | De novo mutations in ATAD3A (ATPase family AAA-domain containing protein 3A) were recently found to cause a neurological syndrome with developmental delay, hypotonia, spasticity, optic atrophy, axonal neuropathy, and hypertrophic cardiomyopathy. Using whole-exome sequencing, we identified a dominantly inherited heterozygous variant c.1064G > A (p.G355D) in ATAD3A in a mother presenting with hereditary spastic paraplegia (HSP) and axonal neuropathy and her son with dyskinetic cerebral palsy, both with disease onset in childhood. HSP is a clinically and genetically heterogeneous disorder of the upper motor neurons. Symptoms beginning in early childhood may resemble spastic cerebral palsy. The function of ATAD3A, a mitochondrial inner membrane AAA ATPase, is yet undefined. AAA ATPases form hexameric rings, which are catalytically dependent on the co-operation of the subunits. The dominant-negative patient mutation affects the Walker A motif, which is responsible for ATP binding in the AAA module of ATAD3A, and we show that the recombinant mutant ATAD3A protein has a markedly reduced ATPase activity. We further show that overexpression of the mutant ATAD3A fragments the mitochondrial network and induces lysosome mass. Similarly, we observed altered dynamics of the mitochondrial network and increased lysosomes in patient fibroblasts and neurons derived through differentiation of patient-specific induced pluripotent stem cells. These alterations were verified in patient fibroblasts to associate with upregulated basal autophagy through mTOR inactivation, resembling starvation. Mutations in ATAD3A can thus be dominantly inherited and underlie variable neurological phenotypes, including HSP, with intrafamiliar variability. This finding extends the group of mitochondrial inner membrane AAA proteins associated with spasticity. |
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| AbstractList | De novo mutations in ATAD3A (ATPase family AAA-domain containing protein 3A) were recently found to cause a neurological syndrome with developmental delay, hypotonia, spasticity, optic atrophy, axonal neuropathy, and hypertrophic cardiomyopathy. Using whole-exome sequencing, we identified a dominantly inherited heterozygous variant c.1064G > A (p.G355D) in ATAD3A in a mother presenting with hereditary spastic paraplegia (HSP) and axonal neuropathy and her son with dyskinetic cerebral palsy, both with disease onset in childhood. HSP is a clinically and genetically heterogeneous disorder of the upper motor neurons. Symptoms beginning in early childhood may resemble spastic cerebral palsy. The function of ATAD3A, a mitochondrial inner membrane AAA ATPase, is yet undefined. AAA ATPases form hexameric rings, which are catalytically dependent on the co-operation of the subunits. The dominant-negative patient mutation affects the Walker A motif, which is responsible for ATP binding in the AAA module of ATAD3A, and we show that the recombinant mutant ATAD3A protein has a markedly reduced ATPase activity. We further show that overexpression of the mutant ATAD3A fragments the mitochondrial network and induces lysosome mass. Similarly, we observed altered dynamics of the mitochondrial network and increased lysosomes in patient fibroblasts and neurons derived through differentiation of patient-specific induced pluripotent stem cells. These alterations were verified in patient fibroblasts to associate with upregulated basal autophagy through mTOR inactivation, resembling starvation. Mutations in ATAD3A can thus be dominantly inherited and underlie variable neurological phenotypes, including HSP, with intrafamiliar variability. This finding extends the group of mitochondrial inner membrane AAA proteins associated with spasticity. |
| Author | Lin, Kai-Lan Tyynismaa, Henna Cooper, Helen M Wanrooij, Sjoerd Lönnqvist, Tuula Khairullin, Rafil Wolf, Alexander Yang, Yang Euro, Liliya Ylikallio, Emil Isohanni, Pirjo Trokovic, Ras Palin, Eino Kaakkola, Seppo Auranen, Mari Woldegebriel, Rosa |
| Author_xml | – sequence: 1 givenname: Helen M surname: Cooper fullname: Cooper, Helen M organization: Åbo Akademi University, Faculty of Natural Sciences and Technology, Turku, Finland – sequence: 2 givenname: Yang surname: Yang fullname: Yang, Yang organization: Institute of Neuroscience, Zhejiang University School of Medicine, Hangzhou, P.R. China – sequence: 3 givenname: Emil surname: Ylikallio fullname: Ylikallio, Emil organization: Clinical Neurosciences, Neurology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland – sequence: 4 givenname: Rafil surname: Khairullin fullname: Khairullin, Rafil organization: Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, Kazan, Russia – sequence: 5 givenname: Rosa surname: Woldegebriel fullname: Woldegebriel, Rosa organization: Research Programs Unit, Molecular Neurology, University of Helsinki, Helsinki, Finland – sequence: 6 givenname: Kai-Lan surname: Lin fullname: Lin, Kai-Lan organization: Åbo Akademi University, Faculty of Natural Sciences and Technology, Turku, Finland – sequence: 7 givenname: Liliya surname: Euro fullname: Euro, Liliya organization: Research Programs Unit, Molecular Neurology, University of Helsinki, Helsinki, Finland – sequence: 8 givenname: Eino surname: Palin fullname: Palin, Eino organization: Research Programs Unit, Molecular Neurology, University of Helsinki, Helsinki, Finland – sequence: 9 givenname: Alexander surname: Wolf fullname: Wolf, Alexander organization: Institute of Molecular Toxicology and Pharmacology, Helmholtz-Zentrum Muenchen-German Research Center for Environmental Health, Neuherberg, Germany – sequence: 10 givenname: Ras surname: Trokovic fullname: Trokovic, Ras organization: Research Programs Unit, Molecular Neurology, University of Helsinki, Helsinki, Finland – sequence: 11 givenname: Pirjo surname: Isohanni fullname: Isohanni, Pirjo organization: Department of Child Neurology, Children's Hospital, Helsinki University Hospital, Helsinki, Finland – sequence: 12 givenname: Seppo surname: Kaakkola fullname: Kaakkola, Seppo organization: Clinical Neurosciences, Neurology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland – sequence: 13 givenname: Mari surname: Auranen fullname: Auranen, Mari organization: Clinical Neurosciences, Neurology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland – sequence: 14 givenname: Tuula surname: Lönnqvist fullname: Lönnqvist, Tuula organization: Department of Child Neurology, Children's Hospital, Helsinki University Hospital, Helsinki, Finland – sequence: 15 givenname: Sjoerd surname: Wanrooij fullname: Wanrooij, Sjoerd organization: Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden – sequence: 16 givenname: Henna surname: Tyynismaa fullname: Tyynismaa, Henna organization: Department of Medical and Clinical Genetics, University of Helsinki, Helsinki, Finland |
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| SubjectTerms | Adenosine Triphosphatases - biosynthesis Adenosine Triphosphatases - genetics Adolescent Adult ATPases Associated with Diverse Cellular Activities Axons - metabolism Axons - pathology Cerebral Palsy - genetics Cerebral Palsy - pathology Child, Preschool Female Gene Expression Regulation Humans Male Membrane Proteins - biosynthesis Membrane Proteins - genetics Mitochondria - metabolism Mitochondria - pathology Mitochondrial Dynamics - genetics Mitochondrial Membranes - metabolism Mitochondrial Membranes - pathology Mitochondrial Proteins - biosynthesis Mitochondrial Proteins - genetics Mutation Spastic Paraplegia, Hereditary - genetics Spastic Paraplegia, Hereditary - pathology TOR Serine-Threonine Kinases - genetics |
| Title | ATPase-deficient mitochondrial inner membrane protein ATAD3A disturbs mitochondrial dynamics in dominant hereditary spastic paraplegia |
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