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Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria
Open accessAbstract
Significance: Selective autophagy of damaged mitochondria (mitophagy) requires protein kinases PINK1 and TBK1, ubiquitin ligase Parkin, and autophagy receptors such as OPTN, driving ubiquitin-labeled mitochondria into autophagosomes. Because all proteins have been genetically linked to either Parkinson’s disease (PINK1 and Parkin) or amyotrophic lateral sclerosis and frontotemporal lobar degeneration (TBK1 and OPTN), it is of great interest to understand their physiological functions. By utilizing quantitative proteomics we show that TBK1 phosphorylates four receptors on several autophagy-relevant sites. Constitutive interaction of TBK1 with OPTN and the ability of OPTN to bind to ubiquitin chains are essential for TBK1 recruitment and activation on mitochondria. TBK1-mediated phosphorylation of OPTN creates a signal amplification loop through combining recruitment and retention of OPTN/TBK1 on ubiquitinated mitochondria.
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“Through its phosphorylation of the autophagy receptors OPTN, SQSTM1, and CALCOCO2/NDP52 (calcium binding and coiled-coil domain 2) [58,59,194], TBK1 regulates several aspects of autophagy, including macroautophagy, xenophagy and mitophagy [59,90,148,194–196].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [194]
In the citing paper
“OPTN is an autophagy receptor that binds ubiquitinated cargo (via its UBAN domain) and LC3 (via its LIR domain) [194,254,255], although it can also act independently of target ubiquitination [254].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [194]
In the citing paper
“Mitochondrial protein ubiquitination promotes mitochondrial recruitment of autophagy regulators and receptors such as TBK1 and optineurin (Heo et al., 2015, Matsumoto et al., 2015, Richter et al., 2016).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Richter et al., 2016
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InfluentialGenetics of primary open-angle glaucoma
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BackgroundThe ketogenic diet and hypoxia promote mitophagy in the context of glaucoma
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Normal-Tension Glaucoma: Epidemiology, Pathogenesis, Diagnosis and Treatment. Review. Part 1
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Rab14 promotes Parkin-mediated mitophagy
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“TBK1 phosphorylates OPTN and is a crucial component of Parkin-OPTN–mediated mitophagy (Richter et al. , 2016; Heo et al. , 2018).”
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“TBK1 constitutively associates with OPTN and is thereby recruited to ubiquitinated mitochondria via OPTN binding [22].”
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“The impaired recruitment of these adap - tors, particularly as a result of TBK1 or OPTN mutations, is significant (Richter et al. 2016).”
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“Subsequently, polyubiquitin chains are recognized by ubiquitin - binding mito-phagy receptors such as OPTN, leading to the engulfment of damaged mitochondria by autophagosomes (35 , 36 , 38 , 39 ).”
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BackgroundInfluentialMitochondrial Function and Dysfunction in White Adipocytes and Therapeutic Implications
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Theme 3 In vitro experimental models
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BackgroundEspina, Á. G. (2022) · Preprints.org · doi:10.20944/preprints202202.0013.v1
“OPTN suppression caused neuronal cell death through the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-Κb) pathway [115].”
BackgroundMinimized combinatorial CRISPR screens identify genetic interactions in autophagy
Diehl, V. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.67332 · Cited by 1
Vacchiano, V., Palombo, F., Ormanbekova, D., Fiorini, C., Fiorentino, A., Caporali, L., Mastrangelo, A., Valentino, M. L., Capellari, S., Liguori, R., et al. (2023) · Preprints.org · doi:10.20944/preprints202307.1739.v1 · Cited by 1
A proteome-wide biochemical screen defines binding determinants of the core autophagy protein LC3BPreprint
Kosmatka, J., Liu, C., Halpin, J. C., Lim, D., Davis, J. H., & Keating, A. E. (2026) · eLife · doi:10.7554/elife.110318.1 · Cited by 2
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Mechanistic insight into the interactions of NAP1 with NDP52 and TAX1BP1 for the recruitment of TBK1Preprint
Fu, T., Liu, J., Wang, Y., Xie, X., Hu, S., & Pan, L. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/264085
“…NDP52/NAP1 or TAX1BP1/NAP1 complex Recent studies reported that the TBK1 kinase can directly or indirectly mediate the phosphorylation of the T39 and S120 residues of NDP52 as well as the S25 residue of TAX1BP1, all of which are within the SKICH region of these two proteins (Richter et al, 2016).”
BackgroundInfluentialSkeletal muscle mitochondrial clearance
Leermakers (2019) · Research Publications (Maastricht University) · doi:10.26481/dis.20190405pl
Mechanisms and Roles of Mitophagy
Vigié, P., Bhatia‐Kiššová, I., & Camougrand, N. M. (2017) · Wiley eBooks · doi:10.1002/9780470015902.a0027587
Kv3.3 Potassium Channels Activate the TBK1 Signaling PathwayPreprint
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Regulation of thermogenesis in Brown and Beige Adipose Tissues
He, C. (2020) · American Journal of Biomedical Science & Research · doi:10.34297/ajbsr.2020.08.001328
“Next, selective autophagy adaptor proteins including nuclear dot protein (NDP52), optineurin (OTEN) and SQSTM1/p62 form autophagy receptors and link the ubiquitinated protein to microtubule-associated protein 1 light chain 3 (LC3) on the outer membrane to turn on mitophagy to clear the excess and damaged mitochondria…”
BackgroundRegulation of intracellular traffic by TBK1 and its relevance to ALS
Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)
Wiggs, J. L. (2020) · Springer eBooks · doi:10.1007/978-3-319-90495-5_165-1
NAK associated protein 1/NAP1 is required for mitosis and cytokinesis by activating TBK1Preprint
Paul, S., Sarraf, S. A., Nam, K. H., Zavar, L., Biswas, S. R., Fritsch, L. E., DeFoor, N., Yaron, T. M., Johnson, J. L., Huntsman, E. M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.09.483647
“signaling, OPTN, TAX1BP1, and NDP52 [21, 30-32] can activate TBK1 during mitophagy.”
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Optineurin is involved in regulating macrophage responses during mycobacterial infectionPreprint
Ramachandran, G., Yeruva, C. V., Swarup, G., & Raghunand, T. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.11.557134
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BackgroundMitochondria and Energy Metabolism in the Pathogenesis and Therapy of Amyotrophic Lateral Sclerosis
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The genetic puzzle of a SOD1-patient with ocular ptosis and a motor neuron disease: a case report
Vacchiano, V., Palombo, F., Ormanbekova, D., Fiorini, C., Fiorentino, A., Caporali, L., Mastrangelo, A., Valentino, M. L., Capellari, S., Liguori, R., et al. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1322067
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PEX14 functions as a molecular link between optineurin and pexophagy in human cellsPreprint
Li, H., Chen, S., Lismont, C., Vandewinkel, B., Hussein, M. A. F., Costa, C. F., Imberechts, D., Liu, Y., Azevedo, J. E., Vandenberghe, W., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.31.596776
Gene Therapy for Neurodegeneration in Glaucoma
Karl, J. J., & Tseng, H. C. (2024) · Essentials in ophthalmology/Essentials ophthalmology · doi:10.1007/978-981-99-4436-1_21
Ktistakis, N. T. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00001-6
Ubiquitin ligase ITCH regulates life cycle of SARS-CoV-2 virus
Xiang, Q., Wouters, C., Chang, P., Lu, Y., Liu, M., Wang, H., Heine, H., Qian, S., Yang, J., Pekosz, A. S., et al. (2026) · eLife · doi:10.7554/elife.105105.3
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Ubiquitin ligase ITCH regulates life cycle of SARS-CoV-2 virusPreprint
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Ubiquitin Ligase ITCH Regulates Life Cycle of SARS-CoV-2 VirusPreprint
Xiang, Q., Wouters, C., Chang, P., Lu, Y., Liu, M., Wang, H., Yang, J., Pekosz, A. S., Zhang, Y., & Wang, J. (2025) · eLife · doi:10.7554/elife.105105.1
Parkin-dependent ubiquitination of TAX1BP1 affects the degradation pathway of defective mitochondriaPreprint
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Autophagy and Neurodegenerative Diseases
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Mechanisms of Autophagy and Its Dysregulation in Neurodegenerative Diseases
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Metadata
- Authors
- Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., Youle, R. J., & Dikic, I.
- Affiliations
- Goethe University Frankfurt (DE)
- National Institutes of Health (US)
- Institute of Molecular Biology (DE)
- University of Vienna (AT)
- Institute of Biochemistry II, Goethe University School of Medicine, 60590 Frankfurt, Germany;
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2016-03-30
- Volume
- 113
- Issue
- 15
- Pages
- 4039-4044
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4839414
- OpenAlex
- W2323582440
- Cited by
- 755
- References
- 44
- Citations by year
- 2026: 64 · 2025: 69 · 2024: 71 · 2023: 56 · 2022: 80 · 2021: 95 · 2020: 82 · 2019: 74 · 2018: 77 · 2017: 60 · 2016: 27
- FWCI
- 74.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (DI 931/3-1)
- Cluster of Excellence (EXC115)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- optineurin, TBK1, phosphorylation, selective autophagy, mitophagy, damaged mitochondria, ubiquitin chains, autophagy receptors, NDP52, TAX1BP1, p62, PINK1, Parkin, signal amplification
- MeSH terms
- Autophagy, HeLa Cells, Humans, Mitochondria, Phosphorylation, Protein Binding, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Ubiquitin, Membrane Transport Proteins, Transcription Factor TFIIIA
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