Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy

Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mit...

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Published inThe Journal of cell biology Vol. 219; no. 9; p. 1
Main Authors Yamano, Koji, Kikuchi, Reika, Kojima, Waka, Hayashida, Ryota, Koyano, Fumika, Kawawaki, Junko, Shoda, Takuji, Demizu, Yosuke, Naito, Mikihiko, Tanaka, Keiji, Matsuda, Noriyuki
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 07.09.2020
Subjects
Activation
Adapters
Adaptor proteins
Animals
Autophagy
Autophagy - physiology
Autophagy-Related Proteins - metabolism
Binding
Biochemistry
Carrier Proteins - metabolism
Cell Cycle Proteins - metabolism
Cell Line, Tumor
Cells, Cultured
Fluorescence
HCT116 Cells
HEK293 Cells
HeLa Cells
Humans
Mammals - metabolism
Mammals - physiology
Membrane Proteins - metabolism
Membrane Transport Proteins - metabolism
Mitochondria
Mitochondria - metabolism
Mitochondria - physiology
Mitophagy
Mitophagy - physiology
Movement disorders
Neurodegenerative diseases
Organelles
Parkin protein
Parkinson's disease
Phagocytosis
Protein Kinases - metabolism
Proteins
PTEN-induced putative kinase
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ubiquitination - physiology
Vesicular Transport Proteins - metabolism
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Abstract Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN–ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria.
AbstractList Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN–ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria.
Damaged mitochondria are selectively eliminated by Parkin/PINK1-mediated autophagy. Kikuchi et al. show that in addition to binding ATG8 proteins, one of the critical autophagy adaptors, OPTN, possesses an ATG9A binding site that contributes to de novo synthesis of autophagosomal membranes. Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN–ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria.
Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson's disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN-ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria.Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson's disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN-ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria.
Author Kikuchi, Reika
Demizu, Yosuke
Kawawaki, Junko
Tanaka, Keiji
Kojima, Waka
Koyano, Fumika
Shoda, Takuji
Yamano, Koji
Naito, Mikihiko
Matsuda, Noriyuki
Hayashida, Ryota
AuthorAffiliation 2 Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan
1 Ubiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan
5 Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Kanagawa, Japan
4 Division of Organic Chemistry, National Institute of Health Sciences, Kanagawa, Japan
3 Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan
AuthorAffiliation_xml – name: 2 Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan
– name: 3 Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan
– name: 1 Ubiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan
– name: 4 Division of Organic Chemistry, National Institute of Health Sciences, Kanagawa, Japan
– name: 5 Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, Kanagawa, Japan
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  orcidid: 0000-0002-4692-161X
  surname: Yamano
  fullname: Yamano, Koji
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  orcidid: 0000-0001-8199-952X
  surname: Matsuda
  fullname: Matsuda, Noriyuki
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32556086$$D View this record in MEDLINE/PubMed
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PublicationDate 2020-09-07
PublicationDateYYYYMMDD 2020-09-07
PublicationDate_xml – month: 09
  year: 2020
  text: 2020-09-07
  day: 07
PublicationDecade 2020
PublicationPlace United States
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– name: New York
PublicationTitle The Journal of cell biology
PublicationTitleAlternate J Cell Biol
PublicationYear 2020
Publisher Rockefeller University Press
Publisher_xml – name: Rockefeller University Press
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Snippet Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin...
Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson's disease, amplify ubiquitin...
Damaged mitochondria are selectively eliminated by Parkin/PINK1-mediated autophagy. Kikuchi et al. show that in addition to binding ATG8 proteins, one of the...
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StartPage 1
SubjectTerms Activation
Adapters
Adaptor proteins
Animals
Autophagy
Autophagy - physiology
Autophagy-Related Proteins - metabolism
Binding
Biochemistry
Carrier Proteins - metabolism
Cell Cycle Proteins - metabolism
Cell Line, Tumor
Cells, Cultured
Fluorescence
HCT116 Cells
HEK293 Cells
HeLa Cells
Humans
Mammals - metabolism
Mammals - physiology
Membrane Proteins - metabolism
Membrane Transport Proteins - metabolism
Mitochondria
Mitochondria - metabolism
Mitochondria - physiology
Mitophagy
Mitophagy - physiology
Movement disorders
Neurodegenerative diseases
Organelles
Parkin protein
Parkinson's disease
Phagocytosis
Protein Kinases - metabolism
Proteins
PTEN-induced putative kinase
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ubiquitination - physiology
Vesicular Transport Proteins - metabolism
Title Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy
URI https://www.ncbi.nlm.nih.gov/pubmed/32556086
https://www.proquest.com/docview/2435541713
https://www.proquest.com/docview/2415286928
https://pubmed.ncbi.nlm.nih.gov/PMC7480101
Volume 219
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