Mitochondrial Dysfunction in Spinocerebellar Ataxia Type 3 Is Linked to VDAC1 Deubiquitination
Dysfunctional mitochondria are linked to several neurodegenerative diseases. Metabolic defects, a symptom which can result from dysfunctional mitochondria, are also present in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease, the most frequent, dominantly inherited neurodeg...
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| Veröffentlicht in: | International journal of molecular sciences 2022-05, Vol.23 (11), p.5933 |
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| creator | Harmuth, Tina Weber, Jonasz J Zimmer, Anna J Sowa, Anna S Schmidt, Jana Fitzgerald, Julia C Schöls, Ludger Riess, Olaf Hübener-Schmid, Jeannette |
| description | Dysfunctional mitochondria are linked to several neurodegenerative diseases. Metabolic defects, a symptom which can result from dysfunctional mitochondria, are also present in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease, the most frequent, dominantly inherited neurodegenerative ataxia worldwide. Mitochondrial dysfunction has been reported for several neurodegenerative disorders and ataxin-3 is known to deubiquitinylate parkin, a key protein required for canonical mitophagy. In this study, we analyzed mitochondrial function and mitophagy in a patient-derived SCA3 cell model. Human fibroblast lines isolated from SCA3 patients were immortalized and characterized. SCA3 patient fibroblasts revealed circular, ring-shaped mitochondria and featured reduced OXPHOS complexes, ATP production and cell viability. We show that wildtype ataxin-3 deubiquitinates VDAC1 (voltage-dependent anion channel 1), a member of the mitochondrial permeability transition pore and a parkin substrate. In SCA3 patients, VDAC1 deubiquitination and parkin recruitment to the depolarized mitochondria is inhibited. Increased p62-linked mitophagy, autophagosome formation and autophagy is observed under disease conditions, which is in line with mitochondrial fission. SCA3 fibroblast lines demonstrated a mitochondrial phenotype and dysregulation of parkin-VDAC1-mediated mitophagy, thereby promoting mitochondrial quality control via alternative pathways. |
| doi_str_mv | 10.3390/ijms23115933 |
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Metabolic defects, a symptom which can result from dysfunctional mitochondria, are also present in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease, the most frequent, dominantly inherited neurodegenerative ataxia worldwide. Mitochondrial dysfunction has been reported for several neurodegenerative disorders and ataxin-3 is known to deubiquitinylate parkin, a key protein required for canonical mitophagy. In this study, we analyzed mitochondrial function and mitophagy in a patient-derived SCA3 cell model. Human fibroblast lines isolated from SCA3 patients were immortalized and characterized. SCA3 patient fibroblasts revealed circular, ring-shaped mitochondria and featured reduced OXPHOS complexes, ATP production and cell viability. We show that wildtype ataxin-3 deubiquitinates VDAC1 (voltage-dependent anion channel 1), a member of the mitochondrial permeability transition pore and a parkin substrate. In SCA3 patients, VDAC1 deubiquitination and parkin recruitment to the depolarized mitochondria is inhibited. Increased p62-linked mitophagy, autophagosome formation and autophagy is observed under disease conditions, which is in line with mitochondrial fission. SCA3 fibroblast lines demonstrated a mitochondrial phenotype and dysregulation of parkin-VDAC1-mediated mitophagy, thereby promoting mitochondrial quality control via alternative pathways.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms23115933</identifier><identifier>PMID: 35682609</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Ataxia ; Ataxin ; Ataxin-3 - genetics ; Ataxin-3 - metabolism ; Autophagy ; Cell viability ; Fibroblasts ; Humans ; Kinases ; Machado-Joseph disease ; Machado-Joseph Disease - genetics ; Machado-Joseph Disease - metabolism ; Membrane permeability ; Microscopy ; Mitochondria ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial DNA ; Mitochondrial permeability transition pore ; Morphology ; Parkin protein ; Parkinson's disease ; Patients ; Phenotypes ; Phosphorylation ; Protein expression ; Proteins ; Quality control ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Voltage-Dependent Anion Channel 1 - genetics ; Voltage-Dependent Anion Channel 1 - metabolism</subject><ispartof>International journal of molecular sciences, 2022-05, Vol.23 (11), p.5933</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3273-734862daf36692d4b16bc59099084890937dc39553fd2b544f1ca12f991122683</citedby><cites>FETCH-LOGICAL-c3273-734862daf36692d4b16bc59099084890937dc39553fd2b544f1ca12f991122683</cites><orcidid>0000-0003-3758-1569 ; 0000-0002-4973-0923</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9180688/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9180688/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35682609$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harmuth, Tina</creatorcontrib><creatorcontrib>Weber, Jonasz J</creatorcontrib><creatorcontrib>Zimmer, Anna J</creatorcontrib><creatorcontrib>Sowa, Anna S</creatorcontrib><creatorcontrib>Schmidt, Jana</creatorcontrib><creatorcontrib>Fitzgerald, Julia C</creatorcontrib><creatorcontrib>Schöls, Ludger</creatorcontrib><creatorcontrib>Riess, Olaf</creatorcontrib><creatorcontrib>Hübener-Schmid, Jeannette</creatorcontrib><title>Mitochondrial Dysfunction in Spinocerebellar Ataxia Type 3 Is Linked to VDAC1 Deubiquitination</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Dysfunctional mitochondria are linked to several neurodegenerative diseases. Metabolic defects, a symptom which can result from dysfunctional mitochondria, are also present in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease, the most frequent, dominantly inherited neurodegenerative ataxia worldwide. Mitochondrial dysfunction has been reported for several neurodegenerative disorders and ataxin-3 is known to deubiquitinylate parkin, a key protein required for canonical mitophagy. In this study, we analyzed mitochondrial function and mitophagy in a patient-derived SCA3 cell model. Human fibroblast lines isolated from SCA3 patients were immortalized and characterized. SCA3 patient fibroblasts revealed circular, ring-shaped mitochondria and featured reduced OXPHOS complexes, ATP production and cell viability. We show that wildtype ataxin-3 deubiquitinates VDAC1 (voltage-dependent anion channel 1), a member of the mitochondrial permeability transition pore and a parkin substrate. In SCA3 patients, VDAC1 deubiquitination and parkin recruitment to the depolarized mitochondria is inhibited. Increased p62-linked mitophagy, autophagosome formation and autophagy is observed under disease conditions, which is in line with mitochondrial fission. SCA3 fibroblast lines demonstrated a mitochondrial phenotype and dysregulation of parkin-VDAC1-mediated mitophagy, thereby promoting mitochondrial quality control via alternative pathways.</description><subject>Ataxia</subject><subject>Ataxin</subject><subject>Ataxin-3 - genetics</subject><subject>Ataxin-3 - metabolism</subject><subject>Autophagy</subject><subject>Cell viability</subject><subject>Fibroblasts</subject><subject>Humans</subject><subject>Kinases</subject><subject>Machado-Joseph disease</subject><subject>Machado-Joseph Disease - genetics</subject><subject>Machado-Joseph Disease - metabolism</subject><subject>Membrane permeability</subject><subject>Microscopy</subject><subject>Mitochondria</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial DNA</subject><subject>Mitochondrial permeability transition pore</subject><subject>Morphology</subject><subject>Parkin protein</subject><subject>Parkinson's disease</subject><subject>Patients</subject><subject>Phenotypes</subject><subject>Phosphorylation</subject><subject>Protein expression</subject><subject>Proteins</subject><subject>Quality control</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Voltage-Dependent Anion Channel 1 - genetics</subject><subject>Voltage-Dependent Anion Channel 1 - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc1LAzEUxIMoflRvniXgxYPVJG83u7kIpfULKh6sHg3ZbFZTt0lNdsX-93apSvU0D96PYYZB6JCSMwBBzu10FhlQmgqADbRLE8b6hPBsc-3eQXsxTglhwFKxjXYg5TnjROyi5zvbeP3qXRmsqvFoEavW6cZ6h63DD3PrvDbBFKauVcCDRn1ahSeLucGAbyMeW_dmStx4_DQaDCkembaw761trFOdyT7aqlQdzcG39tDj1eVkeNMf31_fDgfjvgaWQT-DJOesVBVwLliZFJQXOhVECJIn-VIhKzWINIWqZEWaJBXVirJKCEoZ4zn00MXKd94WM1Nq45qgajkPdqbCQnpl5d-Ps6_yxX9IQXPC887g5Nsg-PfWxEbObNRda2d8GyXjWcopSZZReuj4Hzr1bXDLeh2VAKcs66jTFaWDjzGY6jcMJbIbTq4Pt8SP1gv8wj9LwRfms5LG</recordid><startdate>20220525</startdate><enddate>20220525</enddate><creator>Harmuth, Tina</creator><creator>Weber, Jonasz J</creator><creator>Zimmer, Anna J</creator><creator>Sowa, Anna S</creator><creator>Schmidt, Jana</creator><creator>Fitzgerald, Julia C</creator><creator>Schöls, Ludger</creator><creator>Riess, Olaf</creator><creator>Hübener-Schmid, Jeannette</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3758-1569</orcidid><orcidid>https://orcid.org/0000-0002-4973-0923</orcidid></search><sort><creationdate>20220525</creationdate><title>Mitochondrial Dysfunction in Spinocerebellar Ataxia Type 3 Is Linked to VDAC1 Deubiquitination</title><author>Harmuth, Tina ; 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Metabolic defects, a symptom which can result from dysfunctional mitochondria, are also present in spinocerebellar ataxia type 3 (SCA3), also known as Machado-Joseph disease, the most frequent, dominantly inherited neurodegenerative ataxia worldwide. Mitochondrial dysfunction has been reported for several neurodegenerative disorders and ataxin-3 is known to deubiquitinylate parkin, a key protein required for canonical mitophagy. In this study, we analyzed mitochondrial function and mitophagy in a patient-derived SCA3 cell model. Human fibroblast lines isolated from SCA3 patients were immortalized and characterized. SCA3 patient fibroblasts revealed circular, ring-shaped mitochondria and featured reduced OXPHOS complexes, ATP production and cell viability. We show that wildtype ataxin-3 deubiquitinates VDAC1 (voltage-dependent anion channel 1), a member of the mitochondrial permeability transition pore and a parkin substrate. In SCA3 patients, VDAC1 deubiquitination and parkin recruitment to the depolarized mitochondria is inhibited. Increased p62-linked mitophagy, autophagosome formation and autophagy is observed under disease conditions, which is in line with mitochondrial fission. SCA3 fibroblast lines demonstrated a mitochondrial phenotype and dysregulation of parkin-VDAC1-mediated mitophagy, thereby promoting mitochondrial quality control via alternative pathways.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>35682609</pmid><doi>10.3390/ijms23115933</doi><orcidid>https://orcid.org/0000-0003-3758-1569</orcidid><orcidid>https://orcid.org/0000-0002-4973-0923</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Ataxia Ataxin Ataxin-3 - genetics Ataxin-3 - metabolism Autophagy Cell viability Fibroblasts Humans Kinases Machado-Joseph disease Machado-Joseph Disease - genetics Machado-Joseph Disease - metabolism Membrane permeability Microscopy Mitochondria Mitochondria - genetics Mitochondria - metabolism Mitochondrial DNA Mitochondrial permeability transition pore Morphology Parkin protein Parkinson's disease Patients Phenotypes Phosphorylation Protein expression Proteins Quality control Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Voltage-Dependent Anion Channel 1 - genetics Voltage-Dependent Anion Channel 1 - metabolism |
| title | Mitochondrial Dysfunction in Spinocerebellar Ataxia Type 3 Is Linked to VDAC1 Deubiquitination |
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