Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria
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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 phosphorylation of the autophagy receptors OPTN, SQSTM1, and CALCOCO2/NDP52, TBK1 regulates macroautophagy, xenophagy and mitophagy.
“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]
OPTN is an autophagy receptor that binds ubiquitinated cargo via its UBAN domain and LC3 via its LIR domain, although it can also act independently of target ubiquitination.
“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]
Mitochondrial protein ubiquitination promotes mitochondrial recruitment of autophagy regulators and receptors such as TBK1 and optineurin.
“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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Diverse Cellular Roles of Autophagy
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ALS Genetics: Gains, Losses, and Implications for Future Therapies
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“, 2015) and degradation of damaged mitochondria (mitophagy) (Heo et al., 2015; Lazarou et al., 2015; Moore and Holzbaur, 2016; Richter et al., 2016; Wong and Holzbaur, 2014; Zachari et al., 2019), further supporting a loss of normal OPTN function in autophagy.”
BackgroundInfluentialPINK1/Parkin-mediated mitophagy in neurodegenerative diseases
Li, J., Yang, D., Li, Z., Zhao, M., Wang, D., Sun, Z., Wen, P., Dai, Y., Gou, F., Ji, Y., et al. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101817 · Cited by 388 · see citing works
Autophagy: An Essential Degradation Program for Cellular Homeostasis and Life
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“For mitophagy, activated TBK1 in response to mitochondrial damage phosphorylates OPTN at Ser473 and Ser513 to increase the binding affinity between OPTN and poly-ubiquitin chains on the damaged mitochondria, resulting in the acceleration of mitophagy [85,86].”
BackgroundWiggs, J. L., & Pasquale, L. R. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx184 · Cited by 380 · see citing works
The emerging, multifaceted role of mitophagy in cancer and cancer therapeutics
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Selective autophagy as a potential therapeutic target for neurodegenerative disorders
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TBK1: a new player in ALS linking autophagy and neuroinflammation
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“Whilst wild-type TBK1 localizes to damaged mitochondria, the E696K mutant exhibited severely reduced colocalization with damaged mitochondria [69].”
BackgroundMechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
Bingol, B., & Sheng, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.015 · Cited by 333 · see citing works
Ubiquitin signaling and autophagy
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“Furthermore, TBK1 kinase mediates the phosphorylation of all five mitophagy receptors, generating a positive signaling loop (78, 79).”
BackgroundPINK1 and Parkin: emerging themes in mitochondrial homeostasis.
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“Furthermore, TBK1 phosphorylation of these receptors enhances interactions between LC3 and ubiquitin [22 ,23].”
Ubiquitin-mediated regulation of autophagy
Chen, R., Chen, Y.-H., & Huang, T.-Y. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0569-y · Cited by 320 · see citing works
Parkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells
Villa, E., Proïcs, E., Rubio‐Patiño, C., Obba, S., Zunino, B., Bossowski, J. P., Rozier, R., Chiche, J., Mondragón, L., Riley, J. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.087 · Cited by 315 · see citing works
“It was recently suggested that optineurin and NDP52 are key cargo adaptors for Parkin-mediated mitophagy (Heo et al., 2015; Lazarou et al., 2015; Richter et al., 2016).”
BackgroundPINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol
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“can trigger autophagosome formation through the recruitment of autophagy receptors [24, 25], although cell free systems do not reveal selective binding of autophagy receptors to phospho-ubiquitin [24–26].”
BackgroundSelf-citationALS Genes in the Genomic Era and their Implications for FTD
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HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKα
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Parkin and mitophagy in cancer
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Role and Mechanisms of Mitophagy in Liver Diseases
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“In spite of limited in vivo mitoph gy studies likely due to the technical challenges, a few s dies of mitophagy has be n reported in mouse heart and muscle [91,92]; kid ey [93]; lu [94] and neurons [95].”
BackgroundSelective Autophagy and Xenophagy in Infection and Disease
Sharma, V., Verma, S., Seranova, E., Sarkar, S., & Kumar, D. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00147 · Cited by 248 · see citing works
“The key player in OPTNmediated selective autophagy is TBK1, which phosphorylates it within LIR domain at Ser-177 and enhances its activity (Richter et al., 2016).”
BackgroundMitophagy in tumorigenesis and metastasis
Poole, L. P., & Macleod, K. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03774-1 · Cited by 250 · see citing works
The cGAS-cGAMP-STING Pathway: A Molecular Link Between Immunity and Metabolism
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“(79) recently found that the cGAS-cGAMP-STING downstream target TBK1 phosphorylated several mitophagy receptors such as optineurin (OPTN) and p62 (SQSTM) at their autophagyrelevant sites, which creates a signal loop amplifying mitophagy (Fig.”
BackgroundMitochondrial dysfunction and mitophagy defect triggered by heterozygous GBA mutations
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The Role of Mitophagy in Innate Immunity
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Autophagy Receptors and Neurodegenerative Diseases
Deng, Z., Purtell, K., Lachance, V., Wold, M. S., Chen, S., & Yue, Z. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.01.001 · Cited by 239 · see citing works
“To signal mitophagy, however, TBK1 phosphorylates OPTN at S473 in the UBA domain, which enhances its binding affinity to Ub chains [26].”
BackgroundDetection and Clearance of Damaged Lysosomes by the Endo-Lysosomal Damage Response and Lysophagy
Papadopoulos, C., & Meyer, H. (2017) · Current Biology · doi:10.1016/j.cub.2017.11.012 · Cited by 230 · see citing works
LC3/GABARAPs drive ubiquitin-independent recruitment of Optineurin and NDP52 to amplify mitophagy
Padman, B. S., Nguyen, T. N., Uoselis, L., Skulsuppaisarn, M., Nguyen, L. K., & Lazarou, M. (2019) · Nature Communications · doi:10.1038/s41467-019-08335-6 · Cited by 234 · see citing works
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Evolving and Expanding the Roles of Mitophagy as a Homeostatic and Pathogenic Process
Gustafsson, Å. B., & Dorn, G. W. (2018) · Physiological Reviews · doi:10.1152/physrev.00005.2018 · Cited by 229 · see citing works
Doblado, L., Lueck, C., Rey, C., Samhan-Arias, A. K., Priéto, I., Stacchiotti, A., & Monsalve, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083903 · Cited by 229 · see citing works
“OPTN mutations are rare but have a great functional impact on autophagy and mitophagy.”
BackgroundInfluentialNeuronal Mitophagy in Neurodegenerative Diseases
Martínez‐Vicente, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00064 · Cited by 216 · see citing works
“TANK binding kinase 1 (TBK1) is a kinase activated by mitochondrial depolarization; it is recruited by the receptors to the mitochondria where it is able to phosphorylate both OPTN and NDP52, thereby enhancing the binding of receptors to UB conjugates (Heo et al., 2015; Richter et al., 2016).”
BackgroundTRIM23 mediates virus-induced autophagy via activation of TBK1
Sparrer, K. M. J., Gableske, S., Zurenski, M. A., Parker, Z. M., Full, F., Baumgart, G. J., Kato, J., Pacheco–Rodriguez, G., Liang, C., Pornillos, O., et al. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0017-2 · Cited by 219 · see citing works
“We found TBK1 and p62, two key molecules in selective autophagy 10,11,19,32 , as major TRIM23 interaction partners (Supplementary Fig.”
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works
“Functionally, phosphorylation of opti-neurin by TBK1 promotes the binding of optineurin to its cargoes such as damaged mitochondria (Heo et al , 2015; Richter et al , 2016).”
A guide to the regulation of selective autophagy receptors
Gubaš, A., & Đikić, I. (2021) · FEBS Journal · doi:10.1111/febs.15824 · Cited by 215 · see citing works
Mechanisms and roles of mitophagy in neurodegenerative diseases
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SARS-CoV-2 ORF10 suppresses the antiviral innate immune response by degrading MAVS through mitophagy
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“PINK1 phosphorylates Ub chains on mitochondria and recruits autophagy receptors, such as NDP52, OPTN, and P62, to induce mitophagy [52, 53].”
BackgroundIorio, R., Celenza, G., & Petricca, S. (2021) · Cells · doi:10.3390/cells11010030 · Cited by 218 · see citing works
RAB7A phosphorylation by TBK1 promotes mitophagy via the PINK-PARKIN pathway
Heo, J.-M., Ordureau, A., Swarup, S., Paulo, J. A., Shen, K., Sabatini, D. M., & Harper, J. W. (2018) · Science Advances · doi:10.1126/sciadv.aav0443 · Cited by 199 · see citing works
“These modifications activate PARKIN-dependent ubiquitylation of numerous MOM proteins by PARKIN through a “feed-forward” mechanism involving both recruitment of cytosolic PARKIN to the MOM via interaction with pS65-Ub and accumulation of pS65-Ub as PARKIN increases the abundance of Ub chains on the MOM (1, 2, 4).”
BackgroundInfluentialAutophagy in cancer development, immune evasion, and drug resistance
Niu, X., You, Q., Hou, K., Tian, Y., Wei, P., Zhu, Y., Gao, B., Ashrafizadeh, M., Aref, A. R., Kalbasi, A., et al. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101170 · Cited by 217 · see citing works
Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy
Yamano, K., Kikuchi, R., Kojima, W., Hayashida, R., Koyano, F., Kawawaki, J., Shoda, T., Demizu, Y., Naito, M., Tanaka, K., et al. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201912144 · Cited by 205 · see citing works
“We first introduced an S473E mutation into hAG-OPTN to maintain the higher Ub-binding ability (Richter et al., 2016).”
Influenza A virus protein PB1-F2 impairs innate immunity by inducing mitophagy
Wang, R., Zhu, Y., Ren, C., Yang, S., Tian, S., Chen, H., Jin, M., & Zhou, H. (2020) · Autophagy · doi:10.1080/15548627.2020.1725375 · Cited by 203 · see citing works
“The mitochondrially targeted PINK1 and the PRKN are well-established synergistic mediators of mitophagy of dysfunctional mitochondria, which relies on the ubiquitination of a number of mitochondrial outer membrane substrates and subsequent docking of autophagy receptors to selectively clear mitochondria [71,81].”
BackgroundModelling amyotrophic lateral sclerosis: progress and possibilities
Damme, P. V., Robberecht, W., & Bosch, L. V. D. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.029058 · Cited by 203 · see citing works
“TBK1 can also phosphorylate OPTN and p62, further supporting their intrinsic connections (Richter et al., 2016).”
Ordureau, A., Paulo, J. A., Zhang, J., An, H., Swatek, K. N., Cannon, J. R., Wan, Q., Komander, D., & Harper, J. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.11.013 · Cited by 198 · see citing works
“mitochondria promote recruitment of Ub-binding autophagy receptors to promote autophagosome assembly and delivery to the lysosome (Heo et al., 2015; Lazarou et al., 2015; Richter et al., 2016; Wong and Holzbaur, 2014).”
BackgroundTruban, D., Hou, X., Caulfield, T. R., Fiesel, F. C., & Springer, W. (2016) · Journal of Parkinson’s Disease · doi:10.3233/jpd-160989 · Cited by 237 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
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“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].”
BackgroundWauters, F., Cornelissen, T., Imberechts, D., Martin, S., Koentjoro, B., Sue, C. M., Vangheluwe, P., & Vandenberghe, W. (2019) · Autophagy · doi:10.1080/15548627.2019.1603548 · Cited by 193 · see citing works
“PRKN, OPTN, CALCOCO2 and TBK1 are all critically involved in both mitophagy and xenophagy [19,38,39,43,51,52], and polymorphisms in PRKN are associated with increased susceptibility to Mycobacterium leprae (M.”
BackgroundShu, F., Han, X., Li, Q.-N., Ren, X., Liu, Z., Hu, B., Wang, H., Wang, H., & Jiang, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01300-8 · Cited by 194 · see citing works
“Meanwhile, phosphorylation of S177 and S513 promotes recruitment and retention of OPTN/TBK1 on ubiquitinated, damaged mitochondria.(161) Moreover, TBK1 can also phosphorylate OPTN at S177 site, which helps to enhance LC3 binding affinity and autophagic clearance of cytosolic salmonella.”
BackgroundS-Nitrosylation Targets GSNO Reductase for Selective Autophagy during Hypoxia Responses in Plants
Zhan, N., Wang, C., Chen, L., Yang, H., Feng, J., Gong, X., Ren, B., Wu, R., Mu, J., Li, Y., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.024 · Cited by 192 · see citing works
Self-citationOrdureau, A., Paulo, J. A., Zhang, W., Ahfeldt, T., Zhang, J., Cohn, E. F., Hou, Z., Heo, J., Rubin, L. L., Sidhu, S. S., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.012 · Cited by 184 · see citing works
“…form of Ub chains that are used to recruit Ub-binding autophagy receptors such as OPTN to the MOM is unclear, with evidence for and against direct involvement of pS65Ub in receptor recruitment (Lazarou et al., 2015; Ordureau et al., 2015; Richter et al., 2016); reviewed in (Harper et al., 2018)).”
InfluentialAssociation Between Autophagy and Neurodegenerative Diseases
Fujikake, N., Shin, M., & Shimizu, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00255 · Cited by 167 · see citing works
“Finally, TBK1 promotes autophagy by phosphorylating both SQSTM1 and OPTN, and ALS-associated mutations in TBK1 reduce its binding affinity with OPTN and decrease the clearance of dysfunctional mitochondria (Richter et al., 2016).”
BackgroundExpanding perspectives on the significance of mitophagy in cancer
Drake, L. E., Springer, M. Z., Poole, L. P., Kim, C., & Macleod, K. F. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.008 · Cited by 190 · see citing works
“How BNIP3L/NIX-dependent mitophagy is mechanistically inhibited in red cells by mtDNA mutations and/or associated ROS accumulation, remains to be determined.”
BackgroundInfluentialMitochondrial function in development and disease
Rossmann, M. P., Dubois, S. M., Agarwal, S., & Zon, L. I. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.048912 · Cited by 191 · see citing works
“D is ea se M o d el s & M ec h an is m s enhanced by its phosphorylation, and TANK binding kinase 1 (TBK1), recently also found to be mutated in a subset of ALS patients (Cirulli et al., 2015), is a relevant kinase (Heo et al., 2015; Moore and Holzbaur, 2016; Richter et al., 2016).”
BackgroundHighly Multiplexed Quantitative Mass Spectrometry Analysis of Ubiquitylomes
Rose, C. M., Isasa, M., Ordureau, A., Prado, M. A., Beausoleil, S. A., Jedrychowski, M. P., Finley, D. J., Harper, J. W., & Gygi, S. P. (2016) · Cell Systems · doi:10.1016/j.cels.2016.08.009 · Cited by 174 · see citing works
“…indicated that autophagy adaptors and other regulatory proteins, in addition to PARKIN, are recruited to mitochondria in response to depolarization (Heo et al.,2015; Lazarou et al.,2015; Richter et al., 2016); but, the full repertoire of proteins recruited to depolarized mitochondria is unknown.”
Backgroundvan Wijk, S. J. L., Fricke, F., Herhaus, L., Gupta, J., Hötte, K., Pampaloni, F., Grumati, P., Kaulich, M., Sou, Y., Komatsu, M., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.66 · Cited by 172 · see citing works
Self-citationInterferon-independent STING signaling promotes resistance to HSV-1 in vivo
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Seabright, A. P., Fine, N. H. F., Barlow, J. P., Lord, S. O., Musa, I., Gray, A., Bryant, J. A., Banzhaf, M., Lavery, G. G., Hardie, D. G., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903051r · Cited by 168 · see citing works
Dual role of USP30 in controlling basal pexophagy and mitophagy
Marcassa, E., Kallinos, A., Jardine, J., Rusilowicz‐Jones, E. V., Martinez, A., Kuehl, S., Islinger, M., Clague, M. J., & Urbé, S. (2018) · The EMBO Reports · doi:10.15252/embr.201745595 · Cited by 158 · see citing works
“Phospho-ubiquitin chains can directly recruit specific autophagy receptors, optineurin and NDP52, which in turn engage the autophagy machinery and nascent autophagic membranes [4,5].”
Targeting mitophagy in neurodegenerative diseases
Antico, O., Thompson, P. W., Hertz, N. T., Muqit, M. M. K., & Parton, L. E. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01105-0 · Cited by 178 · see citing works
“26,164,165).”
- 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
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › 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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