Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli

Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and...

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Published inEMBO molecular medicine Vol. 2; no. 12; pp. 490 - 503
Main Authors Costa, Veronica, Giacomello, Marta, Hudec, Roman, Lopreiato, Raffaele, Ermak, Gennady, Lim, Dmitri, Malorni, Walter, Davies, Kelvin J. A., Carafoli, Ernesto, Scorrano, Luca
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.12.2010
WILEY‐VCH Verlag
EMBO Press
WILEY-VCH Verlag
Subjects
Animals
Apoptosis
Calcineurin
Cell culture
Cell death
Cell Line
Cells, Cultured
Cristae
cristae remodelling
Cytochrome
Cytochrome c
Cytochromes c - metabolism
Dynamin
Dynamins
Experiments
Female
fission
Genes
Genetic analysis
Genomes
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
Humans
Huntingtin
Huntington Disease - genetics
Huntington Disease - metabolism
Huntington Disease - physiopathology
Huntington's disease
Huntingtons disease
Hypersensitivity
Male
Mice
Microscopy, Electron, Transmission
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Mitochondria
Mitochondria - genetics
Mitochondria - physiology
Mitochondria - ultrastructure
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Models, Biological
Morphology
Mutation
Neurodegenerative diseases
Neurons - cytology
Neurons - metabolism
Pathogenesis
Phosphorylation
Polyglutamine diseases
Protein Transport
Proteins
Research Article
Software
Trinucleotide repeat diseases
apoptosis
Huntington's disease
cristae remodelling
mitochondria
fission
Online AccessGet full text

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Abstract Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro‐fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis. See accompanying Closeup by Oliveira and Lightowlers DOI https://doi.org/10.1002/emmm.201000104 .
AbstractList Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro-fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis.
Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro‐fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis. See accompanying Closeup by Oliveira and Lightowlers DOI https://doi.org/10.1002/emmm.201000104 .
Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro-fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis.
Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro‐fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis.See accompanying Closeup by Oliveira and Lightowlers DOI 10.1002/emmm.201000104.
Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple mitochondrial alterations. Here, we show that mitochondrial fragmentation and cristae alterations characterize cellular models of HD and participate in their increased susceptibility to apoptosis. In HD cells, the increased basal activity of the phosphatase calcineurin dephosphorylates the pro‐fission dynamin related protein 1 (Drp1), increasing its mitochondrial translocation and activation, and ultimately leading to fragmentation of the organelle. The fragmented HD mitochondria are characterized by cristae alterations that are aggravated by apoptotic stimulation. A genetic analysis indicates that correction of mitochondrial elongation is not sufficient to rescue the increased cytochrome c release and cell death observed in HD cells. Conversely, the increased apoptosis can be corrected by manoeuvres that prevent fission and cristae remodelling. In conclusion, the cristae remodelling of the fragmented HD mitochondria contributes to their hypersensitivity to apoptosis. See accompanying Closeup by Oliveira and Lightowlers DOI 10.1002/emmm.201000104.
Author Giacomello, Marta
Hudec, Roman
Ermak, Gennady
Malorni, Walter
Lim, Dmitri
Costa, Veronica
Lopreiato, Raffaele
Davies, Kelvin J. A.
Carafoli, Ernesto
Scorrano, Luca
AuthorAffiliation 2 Dulbecco-Telethon Institute Rome, Italy
3 Venetian Institute of Molecular Medicine Padova, Italy
5 Dipartimento del Farmaco, Istituto Superiore di Sanità Roma, Italy
1 Department of Cell Physiology and Medicine, University of Geneva Geneva, Switzerland
4 Ethel Percy Andrus Gerontology Center, Davis School of Gerontology, Division of Molecular and Computational Biology, Department of Biological Sciences, College of Letters, Arts and Sciences, University of Southern California Los Angeles, CA, USA
AuthorAffiliation_xml – name: 1 Department of Cell Physiology and Medicine, University of Geneva Geneva, Switzerland
– name: 5 Dipartimento del Farmaco, Istituto Superiore di Sanità Roma, Italy
– name: 2 Dulbecco-Telethon Institute Rome, Italy
– name: 4 Ethel Percy Andrus Gerontology Center, Davis School of Gerontology, Division of Molecular and Computational Biology, Department of Biological Sciences, College of Letters, Arts and Sciences, University of Southern California Los Angeles, CA, USA
– name: 3 Venetian Institute of Molecular Medicine Padova, Italy
Author_xml – sequence: 1
  givenname: Veronica
  surname: Costa
  fullname: Costa, Veronica
  organization: Department of Cell Physiology and Medicine, University of Geneva, Dulbecco‐Telethon Institute, Venetian Institute of Molecular Medicine
– sequence: 2
  givenname: Marta
  surname: Giacomello
  fullname: Giacomello, Marta
  organization: Venetian Institute of Molecular Medicine
– sequence: 3
  givenname: Roman
  surname: Hudec
  fullname: Hudec, Roman
  organization: Venetian Institute of Molecular Medicine
– sequence: 4
  givenname: Raffaele
  surname: Lopreiato
  fullname: Lopreiato, Raffaele
  organization: Venetian Institute of Molecular Medicine
– sequence: 5
  givenname: Gennady
  surname: Ermak
  fullname: Ermak, Gennady
  organization: Ethel Percy Andrus Gerontology Center, Davis School of Gerontology, Division of Molecular and Computational Biology, Department of Biological Sciences, College of Letters, Arts and Sciences, University of Southern California
– sequence: 6
  givenname: Dmitri
  surname: Lim
  fullname: Lim, Dmitri
  organization: Venetian Institute of Molecular Medicine
– sequence: 7
  givenname: Walter
  surname: Malorni
  fullname: Malorni, Walter
  organization: Dipartimento del Farmaco, Istituto Superiore di Sanità
– sequence: 8
  givenname: Kelvin J. A.
  surname: Davies
  fullname: Davies, Kelvin J. A.
  organization: Ethel Percy Andrus Gerontology Center, Davis School of Gerontology, Division of Molecular and Computational Biology, Department of Biological Sciences, College of Letters, Arts and Sciences, University of Southern California
– sequence: 9
  givenname: Ernesto
  surname: Carafoli
  fullname: Carafoli, Ernesto
  organization: Venetian Institute of Molecular Medicine
– sequence: 10
  givenname: Luca
  surname: Scorrano
  fullname: Scorrano, Luca
  email: luca.scorrano@unige.ch
  organization: Department of Cell Physiology and Medicine, University of Geneva, Dulbecco‐Telethon Institute, Venetian Institute of Molecular Medicine
BackLink https://www.ncbi.nlm.nih.gov/pubmed/21069748$$D View this record in MEDLINE/PubMed
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10.1073/pnas.0808249105
10.1074/jbc.M900639200
10.1016/j.brainresbull.2006.03.013
10.1016/S0896-6273(03)00594-4
10.1038/nature07534
10.1074/jbc.M404105200
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Keywords apoptosis
Huntington's disease
cristae remodelling
mitochondria
fission
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Snippet Huntington's disease (HD), a genetic neurodegenerative disease caused by a polyglutamine expansion in the Huntingtin (Htt) protein, is accompanied by multiple...
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SubjectTerms Animals
Apoptosis
Calcineurin
Cell culture
Cell death
Cell Line
Cells, Cultured
Cristae
cristae remodelling
Cytochrome
Cytochrome c
Cytochromes c - metabolism
Dynamin
Dynamins
Experiments
Female
fission
Genes
Genetic analysis
Genomes
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
Humans
Huntingtin
Huntington Disease - genetics
Huntington Disease - metabolism
Huntington Disease - physiopathology
Huntington's disease
Huntingtons disease
Hypersensitivity
Male
Mice
Microscopy, Electron, Transmission
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Mitochondria
Mitochondria - genetics
Mitochondria - physiology
Mitochondria - ultrastructure
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Models, Biological
Morphology
Mutation
Neurodegenerative diseases
Neurons - cytology
Neurons - metabolism
Pathogenesis
Phosphorylation
Polyglutamine diseases
Protein Transport
Proteins
Research Article
Software
Trinucleotide repeat diseases
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Title Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli
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Volume 2
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