The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates
Open accessAbstract
Summary: Aggregation of misfolded proteins and the associated loss of neurons are considered a hallmark of numerous neurodegenerative diseases. Optineurin is present in protein inclusions observed in various neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), Huntington's disease, Alzheimer's disease, Parkinson's disease, Creutzfeld-Jacob disease and Pick's disease. Optineurin deletion mutations have also been described in ALS patients. However, the role of optineurin in mechanisms of protein aggregation remains unclear. In this report, we demonstrate that optineurin recognizes various protein aggregates via its C-terminal coiled-coil domain in a ubiquitin-independent manner. We also show that optineurin depletion significantly increases protein aggregation in HeLa cells and that morpholino-silencing of the optineurin ortholog in zebrafish causes the motor axonopathy phenotype similar to a zebrafish model of ALS. A more severe phenotype is observed when optineurin is depleted in zebrafish carrying ALS mutations. Furthermore, TANK1 binding kinase 1 (TBK1) is colocalized with optineurin on protein aggregates and is important in clearance of protein aggregates through the autophagy-lysosome pathway. TBK1 phosphorylates optineurin at serine 177 and regulates its ability to interact with autophagy modifiers. This study provides evidence for a ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates as well as additional relevance for TBK1 as an upstream regulator of the autophagic pathway.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [254]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The zebrafish book : a guide for the laboratory use of zebrafish (Danio rerio)
Westerfield, M. (1995) · Medical Entomology and Zoology · Cited by 6,813
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Haine, M. M.-L., & Meeùs, N. (1986) · Cited by 3,464
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
Network organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · cited 2×
“, 2010), defective mitochondria (Novak et al., 2010) and bacteria Salmonella enterica (Thurston”
BackgroundPhosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth
Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., et al. (2011) · Science · doi:10.1126/science.1205405 · Cited by 1,298
A Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,268
Mutations of optineurin in amyotrophic lateral sclerosis
Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265
Cited by
Sorted by citations
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citationThe role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646
Rogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966
The LIR motif – crucial for selective autophagy
Birgisdottir, Å. B., Lamark, T., & Johansen, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.126128 · Cited by 914
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786
Self-citationRichter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755
Regulation of selective autophagy: the p62/SQSTM1 paradigm
Lamark, T., Svenning, S., & Johansen, T. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170035 · Cited by 753
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors
Johansen, T., & Lamark, T. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.016 · Cited by 736
Ubiquitin-Dependent And Independent Signals In Selective Autophagy
Khaminets, A., Behl, C., & Đikić, I. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.010 · Cited by 754
Self-citationProtein aggregation in amyotrophic lateral sclerosis
Blokhuis, A. M., Groen, E. J. N., Koppers, M., van den Berg, L. H., & Pasterkamp, R. J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1125-6 · Cited by 607
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
Kirkin, V., & Rogov, V. V. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.005 · Cited by 536
Mechanisms of Selective Autophagy
Lamark, T., & Johansen, T. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-035530 · Cited by 429
Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System
Kocatürk, N. M., & Gözüaçık, D. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00128 · Cited by 442
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
ALS Genetics: Gains, Losses, and Implications for Future Therapies
Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370
Autophagy in Huntington disease and huntingtin in autophagy
Martin, D. D. O., Ladha, S., Ehrnhoefer, D. E., & Hayden, M. R. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.09.003 · Cited by 357
Development of autophagy inducers in clinical medicine
Levine, B., Packer, M., & Codogno, P. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73938 · Cited by 351
Autophagy and neurodegeneration
Frake, R. A., Ricketts, T., Menzies, F. M., & Rubinsztein, D. C. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73944 · Cited by 332
Targeted protein degradation: advances in drug discovery and clinical practice
Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326
Genetics of amyotrophic lateral sclerosis: an update
Chen, S., Sayana, P., Zhang, X., & Le, W. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-28 · Cited by 344
The Role of the Selective Adaptor p62 and Ubiquitin-Like Proteins in Autophagy
Lippai, M., & Lőw, P. (2014) · BioMed Research International · doi:10.1155/2014/832704 · Cited by 338
Matsumoto, G., Shimogori, T., Hattori, N., & Nukina, N. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv179 · Cited by 317
Rogov, V. V., SUZUKI, H., Marinković, M., Lang, V., Kato, R., Kawasaki, M., Buljubašić, M., Šprung, M., Rogova, N. Y., Wakatsuki, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-01258-6 · Cited by 310
Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins
Klionsky, D. J., & Schulman, B. A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2787 · Cited by 284
Selective 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 255
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 245
Autophagy Induction as a Therapeutic Strategy for Neurodegenerative Diseases
Djajadikerta, A., Keshri, S., Tanasa, M. P., Prestil, R., Ryan, L., & Rubinsztein, D. C. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.035 · Cited by 244
Expanding the ubiquitin code through post‐translational modification
Herhaus, L., & Đikić, I. (2015) · EMBO Reports · doi:10.15252/embr.201540891 · Cited by 240
Lactate Dehydrogenase B Controls Lysosome Activity and Autophagy in Cancer
Brisson, L., Bański, P., Sboarina, M., Dethier, C., Danhier, P., Fontenille, M., Hée, V. F. V., Vazeille, T., Tardy, M., Falces, J., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.08.005 · Cited by 229
Deng, Z., Lim, J., Wang, Q., Purtell, K., Wu, S., Palomo, G. M., Tan, H., Manfredi, G., Zhao, Y., Peng, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1644076 · Cited by 237
Human TBK1: A Gatekeeper of Neuroinflammation
Ahmad, L., Zhang, S.-Y., Casanova, J.-L., & Sancho-Shimizu, V. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.04.006 · Cited by 208
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 227
A guide to the regulation of selective autophagy receptors
Gubaš, A., & Đikić, I. (2021) · FEBS Journal · doi:10.1111/febs.15824 · Cited by 229
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196
Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates
Park, H., Kang, J., & Lee, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093369 · Cited by 217
CCT2 is an aggrephagy receptor for clearance of solid protein aggregates
Ma, X., Lu, C., Chen, Y., Li, S., Ma, N., Tao, X., Li, Y., Wang, J., Zhou, M., Yan, Y., et al. (2022) · Cell · doi:10.1016/j.cell.2022.03.005 · Cited by 209
Autophagy and Its Normal and Pathogenic States in the Brain
Yamamoto, A., & Yue, Z. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014149 · Cited by 204
Therapeutic targeting of autophagy in neurodegenerative and infectious diseases
Rubinsztein, D. C., Bento, C. F., & Deretic, V. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150956 · Cited by 202
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 205
Autophagy: A novel mechanism of chemoresistance in cancers
Li, X., Zhou, Y., Li, Y., Yang, L., Ma, Y., Peng, X., Yang, S., Liu, J., & Li, H. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109415 · Cited by 200
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
“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].”
BackgroundHelgason, E., Phung, Q. T., & Dueber, E. C. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.059 · Cited by 184
Autophagy and mitophagy in ALS
Evans, C. S., & Holzbaur, E. L. F. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.005 · Cited by 185
Myocardial stress and autophagy: mechanisms and potential therapies
Delbridge, L. M. D., Mellor, K. M., TAYLOR, D. J., & Gottlieb, R. A. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.35 · Cited by 177
Autophagy-Regulating microRNAs and Cancer
Gözüaçık, D., Akkoç, Y., Öztürk, D. G., & Koçak, M. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00065 · Cited by 180
Shen, W.-C., Li, H.-Y., Chen, G., Chern, Y., & Tu, P. (2014) · Autophagy · doi:10.4161/auto.36098 · Cited by 171
Autophagy in Cell Life and Cell Death
Anding, A. L., & Baehrecke, E. H. (2015) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2015.07.012 · Cited by 164
Autophagy in bone: Self-eating to stay in balance
Pierrefite‐Carle, V., Santucci‐Darmanin, S., Breuil, V., Camuzard, O., & Carle, G. F. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.08.004 · Cited by 161
RNF34 functions in immunity and selective mitophagy by targeting MAVS for autophagic degradation
He, X., Zhu, Y., Zhang, Y., Geng, Y., Gong, J., Geng, J., Zhang, P., Zhang, X., Liu, N., Peng, Y., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018100978 · Cited by 157
Wold, M. S., Lim, J., Lachance, V., Deng, Z., & Yue, Z. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0141-0 · Cited by 153
Goode, A., Butler, K., Long, J., Cavey, J., Scott, D., Shaw, B., Sollenberger, J., Gell, C., Johansen, T., Oldham, N. J., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1170257 · Cited by 153
Nakazawa, S., Oikawa, D., Ishii, R., Ayaki, T., Takahashi, H., Takeda, H., Ishitani, R., Kamei, K., Takeyoshi, I., Kawakami, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms12547 · Cited by 153
Roles of Autophagy in Elimination of Intracellular Bacterial Pathogens
Jo, E., Yuk, J., Shin, D., & Sasakawa, C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00097 · Cited by 160
Loss of TAX1BP1-Directed Autophagy Results in Protein Aggregate Accumulation in the Brain
Sarraf, S. A., Shah, H. V., Kanfer, G., Pickrell, A. M., Holtzclaw, L. A., Ward, M. E., & Youle, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.041 · Cited by 143
Emerging views of OPTN (optineurin) function in the autophagic process associated with disease
Qiu, Y., Wang, J., Li, H., Yang, B., Wang, J., He, Q., & Weng, Q. (2021) · Autophagy · doi:10.1080/15548627.2021.1908722 · Cited by 143
A role for autophagy in Huntington's disease
Croce, K. R., & Yamamoto, A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.08.010 · Cited by 144
Degradation of engulfed mitochondria is rate-limiting in Optineurin-mediated mitophagy in neurons
Evans, C. S., & Holzbaur, E. L. (2020) · eLife · doi:10.7554/elife.50260 · Cited by 137
“These puncta may represent either the self-association of OPTN or the recruitment of OPTN to other autophagy substrates, such as protein aggregates (Korac et al., 2013).”
BackgroundSIRT 5‐mediated deacetylation of LDHB promotes autophagy and tumorigenesis in colorectal cancer
Shi, L., Yan, H., An, S., Shen, M., Jia, W., Zhang, R., Zhao, L., Huang, G., & Liu, J. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12408 · Cited by 137
Optineurin: A Coordinator of Membrane-Associated Cargo Trafficking and Autophagy
Ryan, T. A., & Tumbarello, D. A. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01024 · Cited by 140
Common Molecular Pathways in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Weishaupt, J. H., Hyman, T., & Đikić, I. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.07.005 · Cited by 130
Huntington’s Disease: Complex Pathogenesis and Therapeutic Strategies
Tong, H., Yang, T., Xu, S., Li, X., Liu, L., Zhou, G., Yang, S., Yin, S., Li, X., & Li, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073845 · Cited by 142
Autophagy in health and disease: From molecular mechanisms to therapeutic target
Lu, G. X., Wang, Y., Shi, Y. P., Zhang, Z., Huang, C., He, W., Wang, C., & Shen, H. (2022) · MedComm · doi:10.1002/mco2.150 · Cited by 135
Zientara‐Rytter, K., & Subramani, S. E. (2019) · Cells · doi:10.3390/cells8010040 · Cited by 128
Significance of optineurin mutations in glaucoma and other diseases
Minegishi, Y., Nakayama, M., Iejima, D., Kawase, K., & Iwata, T. (2016) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2016.08.002 · Cited by 126
Li, F., Xie, X., Wang, Y., Liu, J., Cheng, X., Guo, Y., Gong, Y., Hu, S., & Pan, L. (2016) · Nature Communications · doi:10.1038/ncomms12708 · Cited by 124
Zellner, S., Schifferer, M., & Behrends, C. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.009 · Cited by 119
Emerging roles of E3 ubiquitin ligases in autophagy
Kuang, E., Qi, J., & Ronai, Z. A. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.06.008 · Cited by 125
Autophagosome dynamics in neurodegeneration at a glance
Wong, Y. C., & Holzbaur, E. L. F. (2015) · Journal of Cell Science · doi:10.1242/jcs.161216 · Cited by 117
Riguet, N., Mahul-Mellier, A.-L., Maharjan, N., Burtscher, J., Croisier, M., Knott, G., Hastings, J., Patin, A., Reiterer, V., Farhan, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26684-z · Cited by 118
Li, F., Xu, D., Wang, Y., Zhou, Z., Liu, J., Hu, S., Gong, Y., Yuan, J., & Pan, L. (2018) · Autophagy · doi:10.1080/15548627.2017.1391970 · Cited by 120
Dysfunction of Optineurin in Amyotrophic Lateral Sclerosis and Glaucoma
Toth, R. P., & Atkin, J. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01017 · Cited by 114
Autophagy as a common pathway in amyotrophic lateral sclerosis
Nguyen, D. K. H., Thombre, R., & Wang, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.006 · Cited by 118
Taylor, J. P. (2015) · Neurology · doi:10.1212/wnl.0000000000001862 · Cited by 112
Deneubourg, C., Ramm, M., Smith, L. J., Baron, O., Singh, K., Byrne, S., Duchen, M. R., Gautel, M., Eskelinen, E., Fanto, M., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1943177 · Cited by 115
Svenning, S., & Johansen, T. (2013) · Essays in Biochemistry · doi:10.1042/bse0550079 · Cited by 117
Stress granules at the intersection of autophagy and ALS
Monahan, Z. T., Shewmaker, F. P., & Pandey, U. B. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.022 · Cited by 110
Iron and Neurodegeneration: Is Ferritinophagy the Link?
Biasiotto, G., Lorenzo, D. D., Archetti, S., & Zanella, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9473-y · Cited by 105
Quality Control in Neurons: Mitophagy and Other Selective Autophagy Mechanisms
Evans, C. S., & Holzbaur, E. L. F. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.031 · Cited by 109
Autophagy-Dependent Ferroptosis in Cancer
Chen, F., Cai, X., Kang, R., Liu, J., & Tang, D. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0202 · Cited by 104
Protein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?
Webster, C. P., Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00123 · Cited by 109
Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis
Sundaramoorthy, V., Walker, A. K., Tan, V. X., Fifita, J. A., McCann, E. P., Williams, K. L., Blair, I. P., Guillemin, G. J., Farg, M. A., & Atkin, J. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv126 · Cited by 103
Bansal, M., Moharir, S. C., Sailasree, P., Sirohi, K., Sudhakar, C., Sarathi, D. P., Lakshmi, B. J., Buono, M., Kumar, S., & Swarup, G. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.801944 · Cited by 99
Optineurin: The autophagy connection
Ying, H., & Yue, B. Y. J. T. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.06.029 · Cited by 106
Cellular Functions of Optineurin in Health and Disease
Slowicka, K., Vereecke, L., & Loo, G. (2016) · Trends in Immunology · doi:10.1016/j.it.2016.07.002 · Cited by 99
Markovinović, A., Cimbro, R., Ljutić, T., Križ, J., Rogelj, B., & Munitić, I. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.04.005 · Cited by 95
Freischmidt, A., Müller, K., Ludolph, A. C., Weishaupt, J. H., & Andersen, P. M. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.3712 · Cited by 95
Alternative systems for misfolded protein clearance: life beyond the proteasome
Johnston, H. E., & Samant, R. S. (2020) · FEBS Journal · doi:10.1111/febs.15617 · Cited by 93
Zhou, Z., Liu, J., Fu, T., Wu, P., Peng, C., Gong, X., Wang, Y., Zhang, M., Li, Y., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21874-1 · Cited by 98
Su, X., Broach, J. R., Connor, J. R., Gerhard, G. S., & Simmons, Z. (2014) · Muscle & Nerve · doi:10.1002/mus.24198 · Cited by 94
Autophagosome biogenesis and human health
Kawabata, T., & Yoshimori, T. (2020) · Cell Discovery · doi:10.1038/s41421-020-0166-y · Cited by 102
Autophagy receptor defects and ALS-FTLD
Majcher, V., Goode, A., James, V. H., & Layfield, R. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.01.002 · Cited by 101
Chitranshi, N., Dheer, Y., Abbasi, M., You, Y., Graham, S. L., & Gupta, V. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180419121247 · Cited by 92
RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy
Spang, N., Feldmann, A., Huesmann, H., Bekbulat, F., Schmitt, V., Hiebel, C., Koziollek‐Drechsler, I., Clement, A. M., Moosmann, B., Jung, J., et al. (2014) · Autophagy · doi:10.4161/15548627.2014.994359 · Cited by 96
Self-citationThe multifaceted role of glial cells in amyotrophic lateral sclerosis
Valori, C. F., Brambilla, L., Martorana, F., & Rossi, D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1429-7 · Cited by 88
MicroRNAs as major regulators of the autophagy pathway
Akkoç, Y., & Gözüaçık, D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118662 · Cited by 87
Yang, A., Pantoom, S., & Wu, Y. (2017) · eLife · doi:10.7554/elife.23905 · Cited by 85
Proteostasis impairment in ALS
Ruegsegger, C., & Saxena, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.032 · Cited by 88
Metadata
- Authors
- Korac, J., Schaeffer, V., Kovacevic, I., Clement, A. M., Jungblut, B., Behl, C., Terzic, J., & Dikic, I.
- Affiliations
- Department of Immunology and Medical Genetics, School of Medicine, University of Split, Soltanska 2, 21000 Split, Croatia
- Institute of Biochemistry II and Buchmann Institute for Molecular Life Sciences, School of Medicine, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt (Main), Germany
- Johannes Gutenberg University Mainz (DE)
- Max Planck Institute for Heart and Lung Research (DE)
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2013-01-15
- Volume
- 126
- Issue
- 2
- Pages
- 580-592
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC3654196
- OpenAlex
- W1985484942
- Cited by
- 336
- References
- 54
- Citations by year
- 2026: 6 · 2025: 21 · 2024: 25 · 2023: 15 · 2022: 25 · 2021: 25 · 2020: 35 · 2019: 31 · 2018: 25 · 2017: 26 · 2016: 35 · 2015: 37 · 2014: 20 · 2013: 10
- FWCI
- 15.99
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- optineurin, TBK1, protein aggregation, autophagy-lysosome pathway, coiled-coil domain, neurodegenerative diseases, amyotrophic lateral sclerosis, zebrafish model, TBK1 phosphorylation, protein inclusions
- MeSH terms
- Animals, Autophagy, Disease Models, Animal, HeLa Cells, Humans, Mice, Inbred C57BL, Mice, Transgenic, Phosphorylation, Protein Binding, Zebrafish, Cell Cycle Proteins, Neurodegenerative Diseases, Ubiquitin, Membrane Transport Proteins, Transcription Factor TFIIIA, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
