TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation

Autophagy: Renovation of Cells and Tissues

Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276

Mechanisms of mitophagy

Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969

Selective autophagy mediated by autophagic adapter proteins

Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,788

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369

Phosphorylation 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

Regulation of autophagy by ROS: physiology and pathology

Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263

Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization

Sarraf, S. A., Raman, M., Guarani-Pereira, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,010

Interactions between Autophagy Receptors and Ubiquitin-like Proteins Form the Molecular Basis for Selective Autophagy

Rogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992

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

The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria

Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N., & Randow, F. (2009) · Nature Immunology · doi:10.1038/ni.1800 · Cited by 901

Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation

Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812

p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

Narendra, D. P., Kane, L. A., Hauser, D. N., Fearnley, I. M., & Youle, R. J. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 810

Serine 403 Phosphorylation of p62/SQSTM1 Regulates Selective Autophagic Clearance of Ubiquitinated Proteins

Matsumoto, G., Wada, K., Okuno, M., Kurosawa, M., & Nukina, N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.039 · Cited by 714

TBK-1 Promotes Autophagy-Mediated Antimicrobial Defense by Controlling Autophagosome Maturation

Pilli, M., Arko-Mensah, J., Ponpuak, M., Roberts, E., Master, S., Mandell, M. A., Dupont, N., Ornatowski, W., Jiang, S., Bradfute, S. B., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.015 · Cited by 655

Parkin Mediates Proteasome-dependent Protein Degradation and Rupture of the Outer Mitochondrial Membrane

Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612

Autophagy Inhibition Compromises Degradation of Ubiquitin-Proteasome Pathway Substrates

Korolchuk, V. I., Mansilla, A., Menzies, F. M., & Rubinsztein, D. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.021 · Cited by 610

The ubiquitin ligase parkin mediates resistance to intracellular pathogens

Manzanillo, P. S., Ayres, J. S., Watson, R. O., Collins, A. C., Souza, G., Rae, C. S., Schneider, D. S., Nakamura, K., Shiloh, M. U., & Cox, J. S. (2013) · Nature · doi:10.1038/nature12566 · Cited by 588

Nix Is Critical to Two Distinct Phases of Mitophagy, Reactive Oxygen Species-mediated Autophagy Induction and Parkin-Ubiquitin-p62-mediated Mitochondrial Priming

Ding, W.-X., Ni, H.-M., Li, M., Liao, Y., Chen, X., Stolz, D. B., Dorn, G. W., & Yin, X.-M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.119537 · Cited by 551

Parkin Mediates Nonclassical, Proteasomal-Independent Ubiquitination of Synphilin-1: Implications for Lewy Body Formation

Lim, K. L., Chew, K. C. M., Tan, J. M. M., Wang, C., Chung, K. K. K., Zhang, Y., Tanaka, Y., Smith, W., Engelender, S., Ross, C. A., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4474-04.2005 · Cited by 503

p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria

Okatsu, K., Saisho, K., Shimanuki, M., Nakada, K., Shitara, H., Sou, Y., Kimura, M., Sato, S., Hattori, N., Komatsu, M., et al. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01426.x · Cited by 397 · cited 1×

Parkin and PINK1: much more than mitophagy

Scarffe, L. A., Stevens, D. A., Dawson, V. L., & Dawson, T. M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.004 · Cited by 392

NAK is an IκB kinase-activating kinase

Tojima, Y., Fujimoto, A., Delhase, M., Chen, Y., Hatakeyama, S., Nakayama, K. I., Kaneko, Y. S., Nimura, Y., Motoyama, N., Ikeda, K., et al. (2000) · Nature · doi:10.1038/35008109 · Cited by 375

Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates

Korac, J., Schaeffer, V., Kovacevic, I., Clement, A. M., Jungblut, B., Behl, C., Terzic, J., & Dikic, I. (2013) · Journal of Cell Science · doi:10.1242/jcs.114926 · Cited by 336

Crystal Structure and Mechanism of Activation of TANK-Binding Kinase 1

Larabi, A., Devos, J. M., Ng, S., Nanao, M., Round, A. R., Maniatis, T., & Panne, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.034 · Cited by 253

Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation

Ma, X., Helgason, E., Phung, Q. T., Quan, C. L., Iyer, R. S., Lee, M. W., Bowman, K. K., Starovasnik, M. A., & Dueber, E. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121552109 · Cited by 246

Are the IKKs and IKK-related kinases TBK1 and IKK-ɛ similarly activated?

Chau, T., Gioia, R., Gatot, J., Patrascu, F., Carpentier, I., Chapelle, J.-P., O'Neill, L. A. J., Beyaert, R., Piette, J. G., & Chariot, A. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.01.002 · Cited by 229

SINTBAD, a novel component of innate antiviral immunity, shares a TBK1‐binding domain with NAP1 and TANK

Ryzhakov, G., & Randow, F. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601743 · Cited by 196

Neurodegeneration as a consequence of failed mitochondrial maintenance

Karbowski, M., & Neutzner, A. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0921-0 · Cited by 187

Recent insights into the complexity of Tank‐binding kinase 1 signaling networks: The emerging role of cellular localization in the activation and substrate specificity of TBK1

Helgason, E., Phung, Q. T., & Dueber, E. C. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.059 · Cited by 184

Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma

Morton, S., Hesson, L. B., Peggie, M. W., & Cohen, P. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.047 · Cited by 180

Polyubiquitin Binding to Optineurin Is Required for Optimal Activation of TANK-binding Kinase 1 and Production of Interferon β

Gleason, C. E., Ordureau, A., Gourlay, R., Arthur, J. S. C., & Cohen, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267567 · Cited by 177

Ubiquitin Recognition by the Ubiquitin-associated Domain of p62 Involves a Novel Conformational Switch

Long, J., Gallagher, T. R. A., Cavey, J. R., Sheppard, P. W., Ralston, S. H., Layfield, R., & Searle, M. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704973200 · Cited by 159

Negative regulation of TBK1‐mediated antiviral immunity

Zhao, W. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.052 · Cited by 151

IKK-i and TBK-1 are Enzymatically Distinct from the Homologous Enzyme IKK-2

Kishore, N. N., Huynh, Q. K., Mathialagan, S., Hall, T., Rouw, S., Creely, D., Lange, G., Caroll, J., Reitz, B. A., Donnelly, A. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110474200 · Cited by 138

Functional Dissection of the TBK1 Molecular Network

Goncalves, A., Bürckstümmer, T., Dixit, E., Scheicher, R., Górna, M. W., Karayel, E., Sugar, C., Stukalov, A., Berg, T., Kralovics, R., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023971 · Cited by 136

Toward an integrative view of Optineurin functions

Kachaner, D., Génin, P., Laplantine, E., & Weil, R. (2012) · Cell Cycle · doi:10.4161/cc.20946 · Cited by 99

Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and Its Interaction with Ubiquitin and Polyubiquitin

Walinda, E., Morimoto, D., Sugase, K., Konuma, T., Tochio, H., & Shirakawa, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.555441 · Cited by 78

Protein Kinase CK2 is a Constitutively Active Enzyme that Promotes Cell Survival: Strategies to Identify CK2 Substrates and Manipulate its Activity in Mammalian Cells

Turowec, J. P., Duncan, J. S., French, A. C., Gyenis, L., Denis, N. A. S., Vilk, G., & Litchfield, D. W. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-381298-8.00023-x · Cited by 78

Regulation by mitophagy

Hattori, N., Saiki, S., & Imai, Y. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.012 · Cited by 54

Mechanism and medical implications of mammalian autophagy

Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771

Amyotrophic lateral sclerosis

Hardiman, O. M., Al‐Chalabi, A., Chiò, A., Corr, E. M., Logroscino, G., Robberecht, W., Shaw, P. J., Simmons, Z., & van den Berg, L. H. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.71 · Cited by 2,237

Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance

Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081

The mechanisms and roles of selective autophagy in mammals

Vargas, J. N. S., Hamasaki, M., Kawabata, T., Youle, R. J., & Yoshimori, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00542-2 · Cited by 1,088

The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy

Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906

Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria

Richter, 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

The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy

Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906

TBK1 is ubiquitinated by TRIM5α to assemble mitophagy machinery

Saha, B., Olsvik, H. L., Williams, G. L., Oh, S., Evjen, G., Sjøttem, E., & Mandell, M. A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114294 · Cited by 20

S513 A COMBINATION OF MULTIPLE AUTONOMIC PARAMETERS, RATHER THAN EACH PARAMETER ALONE, YIELDS SIGNIFICANT DIFFERENTIATION BETWEEN HEAT PAIN INTENSITIES

Treister, R., Kliger, M., Zuckerman, G. H., Goor-Aryeh, I., & Eisenberg, E. (2011) · European Journal of Pain Supplements · doi:10.1016/s1754-3207(11)70912-9

Optineurin provides a mitophagy contact site for TBK1 activation

Yamano, K., Sawada, M., Kikuchi, R., Nagataki, K., Kojima, W., Endo, R., Kinefuchi, H., Sugihara, A., Fujino, T., Watanabe, A., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00036-1 · Cited by 68