Mitochondrial Dynamics and Mitochondria-Lysosome Contacts in Neurogenetic Diseases
Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics ge...
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| Published in | Frontiers in neuroscience Vol. 16; p. 784880 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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Frontiers Research Foundation
31.01.2022
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| Abstract | Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics genes are known to cause neurogenetic diseases. To better understand the consequences on the cellular phenotype and pathophysiology of neurogenetic diseases associated with defective mitochondrial dynamics, we have compared the fibroblasts phenotypes of (i) patients carrying pathogenic variants in genes involved in mitochondrial dynamics such as
(also known as
),
,
, and
, and (ii) patients carrying mutated genes that their dysfunction affects mitochondria or induces a mitochondrial phenotype, but that are not directly involved in mitochondrial dynamic network, such as
(encoding frataxin, located in the mitochondrial matrix),
(hyperfission phenotype), and
(enlarged mitochondria phenotype). We identified mitochondrial network alterations in all patients' fibroblasts except for
. Functionally, all fibroblasts showed mitochondrial oxidative stress, without membrane potential abnormalities. The lysosomal area and distribution were abnormal in
,
,
, and
fibroblasts. These lysosomal alterations correlated with mitochondria-lysosome membrane contact sites (MCSs) defects in
exclusively. The study of mitochondrial contacts in all samples further revealed a significant decrease in
fibroblasts. GDAP1 and MFN2 are outer mitochondrial membrane (OMM) proteins and both are related to Charcot-Marie Tooth neuropathy. Here we identified their constitutive interaction as well as MFN2 interaction with LAMP-1. Therefore MFN2 is a new mitochondria-lysosome MCSs protein. Interestingly,
and
fibroblasts carry pathogenic changes that occur in their catalytic domains thus suggesting a functional role of GDAP1 and MFN2 in mitochondria-lysosome MCSs. Finally, we observed starvation-induced autophagy alterations in
,
,
,
, and
fibroblasts. These genes are related to mitochondrial membrane structure or lipid composition, which would associate the OMM with starvation-induced autophagy. In conclusion, the study of mitochondrial dynamics and mitochondria-lysosome axis in a group of patients with different neurogenetic diseases has deciphered common and unique cellular phenotypes of degrading and non-degrading pathways that shed light on pathophysiological events, new biomarkers and pharmacological targets for these disorders. |
|---|---|
| AbstractList | Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics genes are known to cause neurogenetic diseases. To better understand the consequences on the cellular phenotype and pathophysiology of neurogenetic diseases associated with defective mitochondrial dynamics, we have compared the fibroblasts phenotypes of (i) patients carrying pathogenic variants in genes involved in mitochondrial dynamics such as
(also known as
),
,
, and
, and (ii) patients carrying mutated genes that their dysfunction affects mitochondria or induces a mitochondrial phenotype, but that are not directly involved in mitochondrial dynamic network, such as
(encoding frataxin, located in the mitochondrial matrix),
(hyperfission phenotype), and
(enlarged mitochondria phenotype). We identified mitochondrial network alterations in all patients' fibroblasts except for
. Functionally, all fibroblasts showed mitochondrial oxidative stress, without membrane potential abnormalities. The lysosomal area and distribution were abnormal in
,
,
, and
fibroblasts. These lysosomal alterations correlated with mitochondria-lysosome membrane contact sites (MCSs) defects in
exclusively. The study of mitochondrial contacts in all samples further revealed a significant decrease in
fibroblasts. GDAP1 and MFN2 are outer mitochondrial membrane (OMM) proteins and both are related to Charcot-Marie Tooth neuropathy. Here we identified their constitutive interaction as well as MFN2 interaction with LAMP-1. Therefore MFN2 is a new mitochondria-lysosome MCSs protein. Interestingly,
and
fibroblasts carry pathogenic changes that occur in their catalytic domains thus suggesting a functional role of GDAP1 and MFN2 in mitochondria-lysosome MCSs. Finally, we observed starvation-induced autophagy alterations in
,
,
,
, and
fibroblasts. These genes are related to mitochondrial membrane structure or lipid composition, which would associate the OMM with starvation-induced autophagy. In conclusion, the study of mitochondrial dynamics and mitochondria-lysosome axis in a group of patients with different neurogenetic diseases has deciphered common and unique cellular phenotypes of degrading and non-degrading pathways that shed light on pathophysiological events, new biomarkers and pharmacological targets for these disorders. Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics genes are known to cause neurogenetic diseases. To better understand the consequences on the cellular phenotype and pathophysiology of neurogenetic diseases associated with defective mitochondrial dynamics, we have compared the fibroblasts phenotypes of (i) patients carrying pathogenic variants in genes involved in mitochondrial dynamics such as DRP1 (also known as DNM1L), GDAP1, OPA1, and MFN2, and (ii) patients carrying mutated genes that their dysfunction affects mitochondria or induces a mitochondrial phenotype, but that are not directly involved in mitochondrial dynamic network, such as FXN (encoding frataxin, located in the mitochondrial matrix), MED13 (hyperfission phenotype), and CHKB (enlarged mitochondria phenotype). We identified mitochondrial network alterations in all patients’ fibroblasts except for CHKBQ198*/Q198*. Functionally, all fibroblasts showed mitochondrial oxidative stress, without membrane potential abnormalities. The lysosomal area and distribution were abnormal in GDAP1W67L/W67L, DRP1K75E/+, OPA1F570L/+, and FXNR165C/GAA fibroblasts. These lysosomal alterations correlated with mitochondria-lysosome membrane contact sites (MCSs) defects in GDAP1W67L/W67L exclusively. The study of mitochondrial contacts in all samples further revealed a significant decrease in MFN2R104W/+ fibroblasts. GDAP1 and MFN2 are outer mitochondrial membrane (OMM) proteins and both are related to Charcot-Marie Tooth neuropathy. Here we identified their constitutive interaction as well as MFN2 interaction with LAMP-1. Therefore MFN2 is a new mitochondria-lysosome MCSs protein. Interestingly, GDAP1W67L/W67L and MFN2R104W/+ fibroblasts carry pathogenic changes that occur in their catalytic domains thus suggesting a functional role of GDAP1 and MFN2 in mitochondria–lysosome MCSs. Finally, we observed starvation-induced autophagy alterations in DRP1K75E/+, GDAP1W67L/W67L, OPA1F570L/+, MFN2R104W/+, and CHKBQ198*/Q198* fibroblasts. These genes are related to mitochondrial membrane structure or lipid composition, which would associate the OMM with starvation-induced autophagy. In conclusion, the study of mitochondrial dynamics and mitochondria-lysosome axis in a group of patients with different neurogenetic diseases has deciphered common and unique cellular phenotypes of degrading and non-degrading pathways that shed light on pathophysiological events, new biomarkers and pharmacological targets for these disorders. Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics genes are known to cause neurogenetic diseases. To better understand the consequences on the cellular phenotype and pathophysiology of neurogenetic diseases associated with defective mitochondrial dynamics, we have compared the fibroblasts phenotypes of (i) patients carrying pathogenic variants in genes involved in mitochondrial dynamics such as DRP1 (also known as DNM1L ), GDAP1 , OPA1 , and MFN2 , and (ii) patients carrying mutated genes that their dysfunction affects mitochondria or induces a mitochondrial phenotype, but that are not directly involved in mitochondrial dynamic network, such as FXN (encoding frataxin, located in the mitochondrial matrix), MED13 (hyperfission phenotype), and CHKB (enlarged mitochondria phenotype). We identified mitochondrial network alterations in all patients’ fibroblasts except for CHKB Q198*/Q198* . Functionally, all fibroblasts showed mitochondrial oxidative stress, without membrane potential abnormalities. The lysosomal area and distribution were abnormal in GDAP1 W67L/W67L , DRP1 K75E/+ , OPA1 F570L/+ , and FXN R165C/GAA fibroblasts. These lysosomal alterations correlated with mitochondria-lysosome membrane contact sites (MCSs) defects in GDAP1 W67L/W67L exclusively. The study of mitochondrial contacts in all samples further revealed a significant decrease in MFN2 R104W/+ fibroblasts. GDAP1 and MFN2 are outer mitochondrial membrane (OMM) proteins and both are related to Charcot-Marie Tooth neuropathy. Here we identified their constitutive interaction as well as MFN2 interaction with LAMP-1. Therefore MFN2 is a new mitochondria-lysosome MCSs protein. Interestingly, GDAP1 W67L/W67L and MFN2 R104W/+ fibroblasts carry pathogenic changes that occur in their catalytic domains thus suggesting a functional role of GDAP1 and MFN2 in mitochondria–lysosome MCSs. Finally, we observed starvation-induced autophagy alterations in DRP1 K75E/+ , GDAP1 W67L/W67L , OPA1 F570L/+ , MFN2 R104W/+ , and CHKB Q198*/Q198* fibroblasts. These genes are related to mitochondrial membrane structure or lipid composition, which would associate the OMM with starvation-induced autophagy. In conclusion, the study of mitochondrial dynamics and mitochondria-lysosome axis in a group of patients with different neurogenetic diseases has deciphered common and unique cellular phenotypes of degrading and non-degrading pathways that shed light on pathophysiological events, new biomarkers and pharmacological targets for these disorders. Mitochondrial network is constantly in a dynamic and regulated balance of fusion and fission processes, which is known as mitochondrial dynamics. Mitochondria make physical contacts with almost every other membrane in the cell thus impacting cellular functions. Mutations in mitochondrial dynamics genes are known to cause neurogenetic diseases. To better understand the consequences on the cellular phenotype and pathophysiology of neurogenetic diseases associated with defective mitochondrial dynamics, we have compared the fibroblasts phenotypes of (i) patients carrying pathogenic variants in genes involved in mitochondrial dynamics such as DRP1 (also known as DNM1L), GDAP1, OPA1 and MFN2, and (ii) patients carrying mutated genes that their dysfunction affects mitochondria or induces a mitochondrial phenotype, but that are not directly involved in mitochondrial dynamic network, such as FXN (encoding frataxin, located in the mitochondrial matrix), MED13 (hyperfision phenotype) and CHKB (enlarged mitochondria phenotype). We identified mitochondrial network alterations in all patients’ fibroblasts except for CHKBQ198*/Q198*. Functionally, all fibroblasts showed mitochondrial oxidative stress, without membrane potential abnormalities. The lysosomal area and distribution were abnormal in GDAP1W67L/W67L, DRP1K75E/+, OPA1F570L/+ and FXNR165C/GAA fibroblasts. These lysosomal alterations correlated with mitochondria-lysosome membrane contact sites (MCSs) defects in GDAP1W67L/W67L exclusively. The study of mitochondrial contacts in all samples further revealed a significant decrease in MFN2R104W/+ fibroblasts. GDAP1 and MFN2 are outer mitochondrial membrane (OMM) proteins and both are related to Charcot-Marie Tooth neuropathy. Here we identified their constitutive interaction as well as MFN2 interaction with LAMP-1. Therefore MFN2 is a new mitochondria-lysosome MCSs protein. Interestingly, GDAP1W67L/W67L and MFN2R104W/+ fibroblasts carry pathogenic changes that occur in their catalytic domains thus suggesting a functional role of GDAP1 and MFN2 in mitochondria–lysosome MCSs. Finally, we observed starvation-induced autophagy alterations in DRP1K75E/+, GDAP1W67L/W67L, OPA1F570L/+, MFN2R104W/+ and CHKBQ198*/Q198* fibroblasts. These genes are related to mitochondrial membrane structure or lipid composition, which would associate the OMM with starvation-induced autophagy. In conclusion, the study of mitochondrial dynamics and mitochondria-lysosome axis in a group of patients with different neurogenetic diseases has deciphered common and unique cellular phenotypes of degrading and non-degrading pathways that shed light on pathophysiological events, new biomarkers and pharmacological targets for these disorders. |
| Author | Carrera-García, Laura Nascimento, Andrés Palau, Francesc Altisent-Huguet, Anna Natera-de Benito, Daniel Cantarero, Lara Hoenicka, Janet Pijuan, Jordi Díaz-Osorio, Yaiza Ortez, Carlos Expósito-Escudero, Jessica Altimir, Arola |
| AuthorAffiliation | 2 Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER) , Barcelona , Spain 4 Department of Genetic Medicine – IPER, Hospital Sant Joan de Déu , Barcelona , Spain 6 Division of Pediatrics, Faculty of Medicine and Health Sciences, University of Barcelona , Barcelona , Spain 5 Clinic Institute of Medicine and Dermatology (ICMiD), Hospital Clínic , Barcelona , Spain 3 Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu , Barcelona , Spain 1 Laboratory of Neurogenetics and Molecular Medicine – IPER, Institut de Recerca Sant Joan de Déu , Barcelona , Spain |
| AuthorAffiliation_xml | – name: 4 Department of Genetic Medicine – IPER, Hospital Sant Joan de Déu , Barcelona , Spain – name: 3 Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu , Barcelona , Spain – name: 6 Division of Pediatrics, Faculty of Medicine and Health Sciences, University of Barcelona , Barcelona , Spain – name: 1 Laboratory of Neurogenetics and Molecular Medicine – IPER, Institut de Recerca Sant Joan de Déu , Barcelona , Spain – name: 2 Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER) , Barcelona , Spain – name: 5 Clinic Institute of Medicine and Dermatology (ICMiD), Hospital Clínic , Barcelona , Spain |
| Author_xml | – sequence: 1 givenname: Jordi surname: Pijuan fullname: Pijuan, Jordi organization: Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER), Barcelona, Spain – sequence: 2 givenname: Lara surname: Cantarero fullname: Cantarero, Lara organization: Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER), Barcelona, Spain – sequence: 3 givenname: Daniel surname: Natera-de Benito fullname: Natera-de Benito, Daniel organization: Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu, Barcelona, Spain – sequence: 4 givenname: Arola surname: Altimir fullname: Altimir, Arola organization: Laboratory of Neurogenetics and Molecular Medicine - IPER, Institut de Recerca Sant Joan de Déu, Barcelona, Spain – sequence: 5 givenname: Anna surname: Altisent-Huguet fullname: Altisent-Huguet, Anna organization: Laboratory of Neurogenetics and Molecular Medicine - IPER, Institut de Recerca Sant Joan de Déu, Barcelona, Spain – sequence: 6 givenname: Yaiza surname: Díaz-Osorio fullname: Díaz-Osorio, Yaiza organization: Laboratory of Neurogenetics and Molecular Medicine - IPER, Institut de Recerca Sant Joan de Déu, Barcelona, Spain – sequence: 7 givenname: Laura surname: Carrera-García fullname: Carrera-García, Laura organization: Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu, Barcelona, Spain – sequence: 8 givenname: Jessica surname: Expósito-Escudero fullname: Expósito-Escudero, Jessica organization: Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu, Barcelona, Spain – sequence: 9 givenname: Carlos surname: Ortez fullname: Ortez, Carlos organization: Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu, Barcelona, Spain – sequence: 10 givenname: Andrés surname: Nascimento fullname: Nascimento, Andrés organization: Neuromuscular Unit, Department of Pediatric Neurology, Hospital Sant Joan de Déu, Barcelona, Spain – sequence: 11 givenname: Janet surname: Hoenicka fullname: Hoenicka, Janet organization: Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER), Barcelona, Spain – sequence: 12 givenname: Francesc surname: Palau fullname: Palau, Francesc organization: Division of Pediatrics, Faculty of Medicine and Health Sciences, University of Barcelona, Barcelona, Spain |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35177962$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | Copyright © 2022 Pijuan, Cantarero, Natera-de Benito, Altimir, Altisent-Huguet, Díaz-Osorio, Carrera-García, Expósito-Escudero, Ortez, Nascimento, Hoenicka and Palau. 2022. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Copyright © 2022 Pijuan, Cantarero, Natera-de Benito, Altimir, Altisent-Huguet, Díaz-Osorio, Carrera-García, Expósito-Escudero, Ortez, Nascimento, Hoenicka and Palau. 2022 Pijuan, Cantarero, Natera-de Benito, Altimir, Altisent-Huguet, Díaz-Osorio, Carrera-García, Expósito-Escudero, Ortez, Nascimento, Hoenicka and Palau |
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| Keywords | membrane contact sites (MCSs) lysosome mitochondria neurogenetic diseases mitochondrial dynamics |
| Language | English |
| License | Copyright © 2022 Pijuan, Cantarero, Natera-de Benito, Altimir, Altisent-Huguet, Díaz-Osorio, Carrera-García, Expósito-Escudero, Ortez, Nascimento, Hoenicka and Palau. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors share senior authorship This article was submitted to Neurogenomics, a section of the journal Frontiers in Neuroscience Edited by: Aurora Gomez-Duran, Margarita Salas Center for Biological Research, Spanish National Research Council (CSIC), Spain Reviewed by: Dario Ronchi, University of Milan, Italy; Marc Germain, Université du Québec à Trois-Rivières, Canada These authors have contributed equally to this work and share first authorship Present address: Arola Altimir, HIPRA Laboratories S.A., Girona, Spain Anna Altisent-Huguet, Reference Laboratory, Barcelona, Spain |
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| Title | Mitochondrial Dynamics and Mitochondria-Lysosome Contacts in Neurogenetic Diseases |
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