Biallelic Mutations in TBCD, Encoding the Tubulin Folding Cofactor D, Perturb Microtubule Dynamics and Cause Early-Onset Encephalopathy
Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause ne...
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| Published in | American journal of human genetics Vol. 99; no. 4; pp. 962 - 973 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
06.10.2016
Cell Press Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0002-9297 1537-6605 1537-6605 |
| DOI | 10.1016/j.ajhg.2016.08.003 |
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| Abstract | Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD, encoding one of the five co-chaperones required for assembly and disassembly of the αβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble α/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain. |
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| AbstractList | Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD, encoding one of the five co-chaperones required for assembly and disassembly of the αβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble α/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain.Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD, encoding one of the five co-chaperones required for assembly and disassembly of the αβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble α/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain. Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD, encoding one of the five co-chaperones required for assembly and disassembly of the αβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble α/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain. Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD, encoding one of the five co-chaperones required for assembly and disassembly of the aβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble a/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain. Microtubules are dynamic cytoskeletal elements coordinating and supporting a variety of neuronal processes, including cell division, migration, polarity, intracellular trafficking, and signal transduction. Mutations in genes encoding tubulins and microtubule-associated proteins are known to cause neurodevelopmental and neurodegenerative disorders. Growing evidence suggests that altered microtubule dynamics may also underlie or contribute to neurodevelopmental disorders and neurodegeneration. We report that biallelic mutations in TBCD , encoding one of the five co-chaperones required for assembly and disassembly of the αβ-tubulin heterodimer, the structural unit of microtubules, cause a disease with neurodevelopmental and neurodegenerative features characterized by early-onset cortical atrophy, secondary hypomyelination, microcephaly, thin corpus callosum, developmental delay, intellectual disability, seizures, optic atrophy, and spastic quadriplegia. Molecular dynamics simulations predicted long-range and/or local structural perturbations associated with the disease-causing mutations. Biochemical analyses documented variably reduced levels of TBCD, indicating relative instability of mutant proteins, and defective β-tubulin binding in a subset of the tested mutants. Reduced or defective TBCD function resulted in decreased soluble α/β-tubulin levels and accelerated microtubule polymerization in fibroblasts from affected subjects, demonstrating an overall shift toward a more rapidly growing and stable microtubule population. These cells displayed an aberrant mitotic spindle with disorganized, tangle-shaped microtubules and reduced aster formation, which however did not alter appreciably the rate of cell proliferation. Our findings establish that defective TBCD function underlies a recognizable encephalopathy and drives accelerated microtubule polymerization and enhanced microtubule stability, underscoring an additional cause of altered microtubule dynamics with impact on neuronal function and survival in the developing brain. |
| Author | Piermarini, Emanuela Pizzi, Simone Francis, Joshua W. Tartaglia, Marco Chandramouli, Balasubramanian Pfundt, Rolph R. Baas, Frank Ciolfi, Andrea Sferra, Antonella Thiffault, Isabelle Carpentieri, Giovanna Dentici, Maria Lisa Piemonte, Fiorella Koolen, David A. Le Pichon, Jean-Baptiste Farrow, Emily Graham, John M. Saunders, Carol J. Levine, Kara Capuano, Alessandro Bertini, Enrico Chillemi, Giovanni Au, Margaret G. Flex, Elisabetta Niceta, Marcello Douglas, Ganka V. Kahn, Richard A. Ivanova, Anna A. Cecchetti, Serena Haaxma, Charlotte A. Dallapiccola, Bruno |
| AuthorAffiliation | 2 Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy 9 CINECA, SCAI-SuperComputing Applications and Innovation Department, Rome 00185, Italy 3 Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Rome 00161, Italy 8 Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA 16 Department of Genome Analysis, Academic Medical Center, Amsterdam 1105, the Netherlands 4 Center for Pediatric Genomic Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA 17 Department of Human Genetics, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands 1 Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome 00161, Italy 11 Dipartimento di Medicina Sperimentale, Sapienza Università di Roma, Rome 00161, Italy 12 Department of Neurology, Donders Institute for Brain, Cognition and Behaviour, Radboud Universi |
| AuthorAffiliation_xml | – name: 7 Department of Pediatrics, Medical Genetics, Cedars-Sinai Medical Center, Los Angeles, CA 90048, USA – name: 14 GeneDx, Gaithersburg, MD 20877, USA – name: 11 Dipartimento di Medicina Sperimentale, Sapienza Università di Roma, Rome 00161, Italy – name: 12 Department of Neurology, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands – name: 4 Center for Pediatric Genomic Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA – name: 2 Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – name: 16 Department of Genome Analysis, Academic Medical Center, Amsterdam 1105, the Netherlands – name: 5 Department of Pathology and Laboratory Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA – name: 13 Centro di Ricerca per gli alimenti e la nutrizione, CREA, Rome 00178, Italy – name: 6 University of Missouri-Kansas City School of Medicine, Kansas City, MO 64108, USA – name: 3 Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Rome 00161, Italy – name: 17 Department of Human Genetics, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands – name: 10 Scuola Normale Superiore, 56126 Pisa, Italy – name: 1 Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome 00161, Italy – name: 8 Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA – name: 15 Department of Pediatrics, Children’s Mercy Hospitals, Kansas City, MO 64108, USA – name: 9 CINECA, SCAI-SuperComputing Applications and Innovation Department, Rome 00185, Italy |
| Author_xml | – sequence: 1 givenname: Elisabetta surname: Flex fullname: Flex, Elisabetta organization: Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome 00161, Italy – sequence: 2 givenname: Marcello surname: Niceta fullname: Niceta, Marcello organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 3 givenname: Serena surname: Cecchetti fullname: Cecchetti, Serena organization: Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Rome 00161, Italy – sequence: 4 givenname: Isabelle surname: Thiffault fullname: Thiffault, Isabelle organization: Center for Pediatric Genomic Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA – sequence: 5 givenname: Margaret G. surname: Au fullname: Au, Margaret G. organization: Department of Pediatrics, Medical Genetics, Cedars-Sinai Medical Center, Los Angeles, CA 90048, USA – sequence: 6 givenname: Alessandro surname: Capuano fullname: Capuano, Alessandro organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 7 givenname: Emanuela surname: Piermarini fullname: Piermarini, Emanuela organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 8 givenname: Anna A. surname: Ivanova fullname: Ivanova, Anna A. organization: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA – sequence: 9 givenname: Joshua W. surname: Francis fullname: Francis, Joshua W. organization: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA – sequence: 10 givenname: Giovanni surname: Chillemi fullname: Chillemi, Giovanni organization: CINECA, SCAI-SuperComputing Applications and Innovation Department, Rome 00185, Italy – sequence: 11 givenname: Balasubramanian surname: Chandramouli fullname: Chandramouli, Balasubramanian organization: Scuola Normale Superiore, 56126 Pisa, Italy – sequence: 12 givenname: Giovanna surname: Carpentieri fullname: Carpentieri, Giovanna organization: Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome 00161, Italy – sequence: 13 givenname: Charlotte A. surname: Haaxma fullname: Haaxma, Charlotte A. organization: Department of Neurology, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands – sequence: 14 givenname: Andrea surname: Ciolfi fullname: Ciolfi, Andrea organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 15 givenname: Simone surname: Pizzi fullname: Pizzi, Simone organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 16 givenname: Ganka V. surname: Douglas fullname: Douglas, Ganka V. organization: GeneDx, Gaithersburg, MD 20877, USA – sequence: 17 givenname: Kara surname: Levine fullname: Levine, Kara organization: GeneDx, Gaithersburg, MD 20877, USA – sequence: 18 givenname: Antonella surname: Sferra fullname: Sferra, Antonella organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 19 givenname: Maria Lisa surname: Dentici fullname: Dentici, Maria Lisa organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 20 givenname: Rolph R. surname: Pfundt fullname: Pfundt, Rolph R. organization: Department of Neurology, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands – sequence: 21 givenname: Jean-Baptiste surname: Le Pichon fullname: Le Pichon, Jean-Baptiste organization: Department of Pediatrics, Children’s Mercy Hospitals, Kansas City, MO 64108, USA – sequence: 22 givenname: Emily surname: Farrow fullname: Farrow, Emily organization: Center for Pediatric Genomic Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA – sequence: 23 givenname: Frank surname: Baas fullname: Baas, Frank organization: Department of Genome Analysis, Academic Medical Center, Amsterdam 1105, the Netherlands – sequence: 24 givenname: Fiorella surname: Piemonte fullname: Piemonte, Fiorella organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 25 givenname: Bruno surname: Dallapiccola fullname: Dallapiccola, Bruno organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 26 givenname: John M. surname: Graham fullname: Graham, John M. organization: Department of Pediatrics, Medical Genetics, Cedars-Sinai Medical Center, Los Angeles, CA 90048, USA – sequence: 27 givenname: Carol J. surname: Saunders fullname: Saunders, Carol J. organization: Center for Pediatric Genomic Medicine, Children’s Mercy Hospital, Kansas City, MO 64108, USA – sequence: 28 givenname: Enrico surname: Bertini fullname: Bertini, Enrico organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy – sequence: 29 givenname: Richard A. surname: Kahn fullname: Kahn, Richard A. organization: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA – sequence: 30 givenname: David A. surname: Koolen fullname: Koolen, David A. organization: Department of Human Genetics, Donders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 1105, the Netherlands – sequence: 31 givenname: Marco surname: Tartaglia fullname: Tartaglia, Marco email: marco.tartaglia@opbg.net organization: Genetics and Rare Diseases Research Division, Ospedale Pediatrico Bambino Gesù, Rome 00146, Italy |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27666370$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | 2016 American Society of Human Genetics Copyright © 2016 American Society of Human Genetics. Published by Elsevier Inc. All rights reserved. Copyright Cell Press Oct 6, 2016 2016 American Society of Human Genetics. 2016 American Society of Human Genetics |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 These authors contributed equally to this work |
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| Title | Biallelic Mutations in TBCD, Encoding the Tubulin Folding Cofactor D, Perturb Microtubule Dynamics and Cause Early-Onset Encephalopathy |
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