Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death
Open accessAbstract
An intronic expansion of GGGGCC repeats within the C9ORF72 gene is the most common genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia (ALS-FTD). Ataxin-2 with intermediate length of polyglutamine expansions (Ataxin-2 Q30x) is a genetic modifier of the disease. Here, we found that C9ORF72 forms a complex with the WDR41 and SMCR8 proteins to act as a GDP/GTP exchange factor for RAB8a and RAB39b and to thereby control autophagic flux. Depletion of C9orf72 in neurons partly impairs autophagy and leads to accumulation of aggregates of TDP-43 and P62 proteins, which are histopathological hallmarks of ALS-FTD SMCR8 is phosphorylated by TBK1 and depletion of TBK1 can be rescued by phosphomimetic mutants of SMCR8 or by constitutively active RAB39b, suggesting that TBK1, SMCR8, C9ORF72, and RAB39b belong to a common pathway regulating autophagy. While depletion of C9ORF72 only has a partial deleterious effect on neuron survival, it synergizes with Ataxin-2 Q30x toxicity to induce motor neuron dysfunction and neuronal cell death. These results indicate that partial loss of function of C9ORF72 is not deleterious by itself but synergizes with Ataxin-2 toxicity, suggesting a double-hit pathological mechanism in ALS-FTD.
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The C9orf72-SMCR8-WDR41 complex acts as a guanine nucleotide exchange factor for RAB8A and RAB39B, regulating vesicle trafficking and autophagic flux.
“Separately, the C9orf72-SMCR8-WDR41 complex acts as a guanine nucleotide exchange factor for RAB8A and RAB39B, regulating vesicle trafficking and autophagic flux [148].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [148]
C9orf72 forms a complex with SMCR8 and WDR41, which targets the complex to lysosomes and interacts with RB1CC1-ULK1-ATG13-ATG101 to regulate autophagosome formation.
“C9orf72 also forms a complex with SMCR8, a guanine nucleotide exchange factor, and WDR41, a WD40 protein essential for targeting the C9orf72-SMCR8-WDR41 complex to lysosomes [146–150]. Here, this complex interacts with RB1CC1-ULK1-ATG13-ATG101, which together are involved in autophagosome formation [149].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [148]
C9orf72 assists in the formation of nascent autophagosomes, consistent with impaired autophagy observed in murine cortical neurons and human iPSC-derived neurons upon C9orf72 knockdown.
“Together, these findings suggest that C9orf72 assists in the formation of nascent autophagosomes, consistent with the finding of impaired autophagy in murine cortical neurons [148] and human iPSC-derived neurons [154] upon C9orf72 knockdown.”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [148]
TBK1 phosphorylates SMCR8, which forms a complex with C9orf72 and WDR41, thereby enhancing autophagy initiation.
“TBK1 also phosphorylates SMCR8, which forms a complex with C9orf72 and WDR41, thereby enhancing autophagy initiation [148].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [148]
In neurons, TBK1 knockdown enhances the accumulation of SQSTM1, which can be rescued by phosphomimetic SMCR8 mutations, suggesting that SMCR8 phosphorylation is crucial for TBK1's effects on autophagy.
“In neurons, TBK1 knockdown enhances the accumulation of SQSTM1, which can be rescued by phosphomimetic SMCR8 mutations [148], suggesting that SMCR8 phosphorylation is crucial for TBK1’s effects on autophagy.”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [148]
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 [148]
Genetic ablation of C9orf72 correlates with an increased burden of SQSTM1/p62 and TARDBP protein aggregation and synergizes with polyQ ATXN2 to induce the demise of motor neurons.
“Supporting this notion, genetic ablation of C9orf72 correlates with an increased burden of SQSTM1/p62 and TARDBP protein aggregation and synergizes with polyQ ATXN2 to induce the demise of motor neurons (Sellier et al, 2016).”
From Autophagy in major human diseases (2021) · cites this paper as Sellier et al, 2016
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Cites
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · see citing works
A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409 · see citing works
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · see citing works
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · see citing works
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630 · see citing works
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works
Production of monoclonal antibodies: Strategy and tactics
Groth, S., & Scheidegger, D. (1980) · Journal of Immunological Methods · doi:10.1016/0022-1759(80)90146-5 · Cited by 1,581 · see citing works
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 · see citing works
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Velde, C. V., Bouchard, J.-P., Lacomblez, L., Pochigaeva, K., Salachas, F., et al. (2008) · Nature Genetics · doi:10.1038/ng.132 · Cited by 1,544 · see citing works
Self-citationAtaxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
Elden, A. C., Kim, H.-J., Hart, M. P., Chen‐Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R. A., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,327 · see citing works
Phosphorylation of the Autophagy Receptor Optineurin Restricts <i>Salmonella</i> 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 · see citing works
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 · see citing works
The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS
Mori, K., Weng, S., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H. A., Cruts, M., Broeckhoven, C. V., et al. (2013) · Science · doi:10.1126/science.1232927 · Cited by 1,248 · see citing works
Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS
Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235 · see citing works
Majounie, E., Renton, A. E., Mok, K., Dopper, E. G., Waite, A., Rollinson, S., Chiò, A., Restagno, G., Nicolaou, N., Simon-Sanchez, J., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70043-1 · Cited by 1,210 · see citing works
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174 · see citing works
Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2
Pulst, S.-M., Nechiporuk, A. V., Nechiporuk, T., Gispert, S., Chen, X., Lopes‐Cendes, Í., Pearlman, S., Starkman, S., Díaz, G. O., Lunkes, A., et al. (1996) · Nature Genetics · doi:10.1038/ng1196-269 · Cited by 1,113 · see citing works
Hsu, P. P., Kang, S. A., Rameseder, J., Zhang, Y., Ottina, K. A., Lim, D., Peterson, T. R., Choi, Y., Gray, N. S., Yaffe, M. B., et al. (2011) · Science · doi:10.1126/science.1199498 · Cited by 1,084 · see citing works
Ash, P. E. A., Bieniek, K. F., Gendron, T. F., Caulfield, T. R., Lin, W.-L., DeJesus‐Hernandez, M., van Blitterswijk, M., Jansen‐West, K. R., Paul, J. W., Rademakers, R., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.004 · Cited by 1,079 · see citing works
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.
Zhang, K., Donnelly, C. J., Haeusler, A. R., Grima, J. C., Machamer, J. B., Steinwald, P., Daley, E. L., Miller, S. J., Cunningham, K. M., Vidensky, S., et al. (2015) · Nature · doi:10.1038/nature14973 · Cited by 982 · see citing works
C9orf72 nucleotide repeat structures initiate molecular cascades of disease
Haeusler, A. R., Donnelly, C. J., Periz, G., Simko, E. A. J., Shaw, P. G., Kim, M.-S., Maragakis, N. J., Troncoso, J. C., Pandey, A., Sattler, R., et al. (2014) · Nature · doi:10.1038/nature13124 · Cited by 978 · see citing works
FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
Hara, T., Takamura, A., Kishi, C., Iemura, S.-I., Natsume, T., Guan, J., & Mizushima, N. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712064 · Cited by 971 · see citing works
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 · see citing works
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 · see citing works
Autophagy gone awry in neurodegenerative diseases
Wong, E. S. P., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 883 · see citing works
RNA Toxicity from the ALS/FTD C9ORF72 Expansion Is Mitigated by Antisense Intervention
Donnelly, C. J., Zhang, P.-W., Pham, J. T., Haeusler, A. R., Mistry, N. A., Vidensky, S., Daley, E. L., Poth, E. M., Hoover, B., Fines, D. M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.015 · Cited by 877 · see citing works
Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N., & Randow, F. (2009) · Nature Immunology · doi:10.1038/ni.1800 · Cited by 872 · see citing works
Imbert, G., Saudou, F., Yvert, G., Devys, D., Trottier, Y., Garnier, J., Weber, C., Mandel, J., Cancel‐Tassin, G., Abbas, N., et al. (1996) · Nature Genetics · doi:10.1038/ng1196-285 · Cited by 848 · see citing works
Prevalence and patterns of cognitive impairment in sporadic ALS
Ringholz, G. M., Appel, S. H., Bradshaw, M. R., Cooke, N., Mosnik, D. M., & Schulz, P. E. (2005) · Neurology · doi:10.1212/01.wnl.0000172911.39167.b6 · Cited by 843 · see citing works
GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841 · see citing works
Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
Skibinski, G., Parkinson, N. J., Brown, J. M., Chakrabarti, L., Lloyd, S. L., Hummerich, H., Nielsen, J. E., Hodges, J. R., Spillantini, M. G., Thusgaard, T., et al. (2005) · Nature Genetics · doi:10.1038/ng1609 · Cited by 822 · see citing works
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 · see citing works
Sanpei, K., Takano, H., Igarashi, S., Sato, T., Oyake, M., Sasaki, H., Wakisaka, A., Tashiro, K., Ishida, Y., Ikeuchi, T., et al. (1996) · Nature Genetics · doi:10.1038/ng1196-277 · Cited by 763 · see citing works
RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia
Zu, T., Liu, Y., Báñez-Coronel, M., Reid, T. S., Pletniková, O., Lewis, J. M., Miller, T. M., Harms, M. B., Falchook, A. E., Subramony, S. H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315438110 · Cited by 748 · see citing works
Mizielinska, S., Grönke, S., Niccoli, T., Ridler, C. E., Clayton, E. L., Devoy, A., Moens, T., Norona, F. E., Woollacott, I. O. C., Pietrzyk, J., et al. (2014) · Science · doi:10.1126/science.1256800 · Cited by 740 · see citing works
Eukaryotic Stress Granules Are Cleared by Autophagy and Cdc48/VCP Function
Buchan, J. R., Kolaitis, R.-M., Taylor, J. P., & Parker, R. (2013) · Cell · doi:10.1016/j.cell.2013.05.037 · Cited by 737 · see citing works
Van Deerlin, V. M., Leverenz, J. B., Bekris, L. M., Bird, T. D., Yuan, W., Elman, L. B., Clay, D., Wood, E. M., Chen-Plotkin, A. S., Martinez-Lage, M., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70071-1 · Cited by 723 · see citing works
The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
Lomen, C. E., Anderson, T. T., & Miller, B. L. (2002) · Neurology · doi:10.1212/wnl.59.7.1077 · Cited by 699 · see citing works
Sun, N., Yun, J., Liu, J., Malide, D. A., Liu, C., Rovira, I. I., Holmström, K. M., Fergusson, M. M., Yoo, Y. H., Combs, C. A., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.009 · Cited by 696 · see citing works
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 · see citing works
Fecto, F. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.250 · Cited by 650 · see citing works
Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells
Kwon, I., Xiang, S., Kato, M., Wu, L. C., Theodoropoulos, P., Wang, T., Kim, J., Yun, J., Xie, Y., & McKnight, S. L. (2014) · Science · doi:10.1126/science.1254917 · Cited by 648 · see citing works
Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626 · see citing works
Gijselinck, I., Langenhove, T. V., van der Zee, J., Sleegers, K., Philtjens, S., Kleinberger, G., Janssens, J., Bettens, K., Cauwenberghe, C. V., Pereson, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70261-7 · Cited by 626 · see citing works
TDP‐43 A315T mutation in familial motor neuron disease
Gitcho, M. A., Baloh, R. H., Chakraverty, S., Mayo, K., Norton, J. B., Levitch, D., Hatanpaa, K. J., White, C. L., Bigio, E. H., Caselli, R. J., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21344 · Cited by 619 · see citing works
Jovičić, A., Mertens, J., Boeynaems, S., Bogaert, E., Chai, N., Yamada, S. B., Paul, J. W., Sun, S., Herdy, J. R., Bieri, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4085 · Cited by 598 · see citing works
Chaperone-Assisted Selective Autophagy Is Essential for Muscle Maintenance
Arndt, V., Dick, N., Tawo, R., Dreiseidler, M., Wenzel, D., Hesse, M., Fürst, D. O., Säftig, P., Saint, R. B., Fleischmann, B. K., et al. (2010) · Current Biology · doi:10.1016/j.cub.2009.11.022 · Cited by 572 · see citing works
Gendron, T. F., Bieniek, K. F., Zhang, Y., Jansen‐West, K. R., Ash, P. E. A., Caulfield, T. R., Daughrity, L. M., Dunmore, J., Castanedes‐Casey, M., Chew, J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1192-8 · Cited by 569 · see citing works
Tsun, Z.-Y., Bar-Peled, L., Chantranupong, L., Zoncu, R., Wang, T., Kim, C., Spooner, E., & Sabatini, D. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.016 · Cited by 565 · see citing works
Lagier‐Tourenne, C., Baughn, M. W., Rigo, F., Sun, S., Liu, P., Li, H., Jiang, J., Watt, A. T., Chun, S. J., Katz, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318835110 · Cited by 555 · see citing works
Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin
Hu, F., Padukkavidana, T., Vægter, C. B., Brady, O. A., Zheng, Y., Mackenzie, I. R., Feldman, H., Nykjær, A., & Strittmatter, S. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.034 · Cited by 545 · see citing works
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522 · cited 1× · see citing works
“…(BCL2-associated athanogene 3) and the ubiquitin ligase STUB1 (also known as CHIP) to initiate aggrephagy, also named chaperone-assisted selective autophagy (CASA), which is the selective autophagy of chaperone-bound misfolded or aggregated proteins (Gamerdinger et al , 2009; Arndt et al , 2010).”
Wen, X., Tan, W., Westergard, T., Krishnamurthy, K., Markandaiah, S. S., Shi, Y., Lin, S., Shneider, N. A., Monaghan, J., Pandey, U. B., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.12.010 · Cited by 513 · see citing works
Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494 · see citing works
Lee, Y., Chen, H.-J., Peres, J., Gómez-Deza, J., Attig, J., Štalekar, M., Troakes, C., Nishimura, A. L., Scotter, E. L., Vance, C. A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.049 · Cited by 487 · see citing works
Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A. K., Levina, V., Halloran, M. A., Gleeson, P. A., Blair, I. P., Soo, K. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu068 · Cited by 478 · see citing works
Al-Sarraj, S., King, A., Troakes, C., Smith, B., Maekawa, S., Bodi, I., Rogelj, B., Al-Chalabi, A., Hortobágyi, T., & Shaw, C. E. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0911-2 · Cited by 475 · see citing works
siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy
Chan, E. Y. W., Kır, S., & Tooze, S. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703663200 · Cited by 468 · see citing works
Novel Mutations in TARDBP (TDP-43) in Patients with Familial Amyotrophic Lateral Sclerosis
Rutherford, N. J., Zhang, Y., Baker, M. C., Gass, J. M., Finch, N. A., Xu, Y., Stewart, H. G., Kelley, B. J., Kuntz, K., Crook, R., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000193 · Cited by 450 · see citing works
Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
Barmada, S. J., Serio, A., Arjun, A., Bilican, B., Daub, A., Ando, D. M., Tsvetkov, A., Pleiss, M., Li, X., Peisach, D., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1563 · Cited by 431 · see citing works
Hoffman, N. J., Parker, B. L., Chaudhuri, R., Fisher-Wellman, K. H., Kleinert, M., Humphrey, S. J., Yang, P., Holliday, M., Trefely, S., Fazakerley, D. J., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.001 · Cited by 426 · see citing works
Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
Kabashi, E., Lin, L., Tradewell, M. L., Dion, P. A., Bercier, V., Bourgouin, P., Rochefort, D. L., Hadj, S. B., Durham, H. D., Velde, C. V., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp534 · Cited by 416 · see citing works
Self-citationC9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits
Chew, J., Gendron, T. F., Prudencio, M., Sasaguri, H., Zhang, Y., Castanedes‐Casey, M., Lee, C. W., Jansen‐West, K. R., Kurti, A., Murray, M. E., et al. (2015) · Science · doi:10.1126/science.aaa9344 · Cited by 410 · see citing works
Wang, I.-F., Guo, B.-S., Liu, Y.-C., Wu, C.-C., Yang, C.-H., Tsai, K.-J., & Shen, C.-K. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206362109 · Cited by 377 · see citing works
<i>TDP</i> ‐ <i>43</i> mutation in familial amyotrophic lateral sclerosis
Yokoseki, A., Shiga, A., Tan, C., Tagawa, A., Kaneko, H., Koyama, A., Eguchi, H., Tsujino, A., Ikeuchi, T., Kakita, A., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21392 · Cited by 373 · see citing works
Kim, H., Raphael, A. R., LaDow, E., McGurk, L., Weber, R. A., Trojanowski, J. Q., Lee, V. M. ‐., Finkbeiner, S. M., Gitler, A. D., & Bonini, N. M. (2013) · Nature Genetics · doi:10.1038/ng.2853 · Cited by 370 · see citing works
Recruitment of folliculin to lysosomes supports the amino acid–dependent activation of Rag GTPases
Petit, C. S., Roczniak-Ferguson, A., & Ferguson, S. M. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307084 · Cited by 355 · see citing works
Mori, K., Lammich, S., Mackenzie, I. R., Forné, I., Zilow, S., Kretzschmar, H. A., Edbauer, D., Janssens, J., Kleinberger, G., Cruts, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1088-7 · Cited by 339 · see citing works
Evidence for an oligogenic basis of amyotrophic lateral sclerosis
van Blitterswijk, M., van Es, M. A., Hennekam, E. A. M., Dooijes, D., van Rheenen, W., Medic, J., Bourque, P. R., Schelhaas, H. J., van der Kooi, A. J., de Visser, M., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds199 · Cited by 338 · see citing works
Ciura, S., Lattante, S., Le Ber, I., Latouche, M., Tostivint, H., Brice, A., & Kabashi, E. (2013) · Annals of Neurology · doi:10.1002/ana.23946 · Cited by 333 · see citing works
Self-citationZhang, Y., Jansen‐West, K. R., Xu, Y.-F., Gendron, T. F., Bieniek, K. F., Lin, W.-L., Sasaguri, H., Caulfield, T. R., Hubbard, J., Daughrity, L. M., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1336-5 · Cited by 328 · see citing works
Almeida, S., Gascon, E., Tran, H., Chou, H. J., Gendron, T. F., DeGroot, S., Tapper, A. R., Sellier, C., Charlet-Berguerand, N., Karydas, A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1149-y · Cited by 321 · see citing works
Self-citationLevine, T. P., Daniels, R. D., Gatta, A. T., Wong, L. H., & Hayes, M. J. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts725 · Cited by 321 · see citing works
Sequestration of multiple RNA recognition motif-containing proteins by C9orf72 repeat expansions
Cooper‐Knock, J., Walsh, M. J., Higginbottom, A., Highley, J. R., Dickman, M. J., Edbauer, D., Ince, P. G., Wharton, S. B., Wilson, S. A., Kirby, J., et al. (2014) · Brain · doi:10.1093/brain/awu120 · Cited by 320 · see citing works
Mizielinska, S., Lashley, T., Norona, F. E., Clayton, E. L., Ridler, C. E., Fratta, P., & Isaacs, A. M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1200-z · Cited by 317 · see citing works
Matsumoto, G., Shimogori, T., Hattori, N., & Nukina, N. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv179 · Cited by 317 · see citing works
Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., Brown, P., Ravenscroft, T., van Blitterswijk, M., Nicholson, A. M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1436-x · Cited by 312 · see citing works
May, S., Hornburg, D., Schludi, M. H., Arzberger, T., Rentzsch, K., Schwenk, B. M., Grässer, F. A., Mori, K., Kremmer, E., Banzhaf‐Strathmann, J., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1329-4 · Cited by 302 · see citing works
C9orf72 BAC Transgenic Mice Display Typical Pathologic Features of ALS/FTD
O’Rourke, J. G., Bogdanik, L., Muhammad, A. K. M. G., Gendron, T. F., Kim, K. J., Austin, A., Cady, J., Liu, E. Y., Zarrow, J., Grant, S., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.027 · Cited by 298 · see citing works
Waite, A. J., Bäumer, D., East, S. Z., Neal, J., Morris, H. R., Ansorge, O., & Blake, D. J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.016 · Cited by 277 · see citing works
Wilson, G. R. A., Sim, J. C. H., McLean, C., Giannandrea, M., Galea, C. A., Riseley, J. R., Stephenson, S. E. M., Fitzpatrick, E., Haas, S. A., Pope, K., et al. (2014) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.10.015 · Cited by 273 · see citing works
C 9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits
Koppers, M., Blokhuis, A. M., Westeneng, H., Terpstra, M. L., Zundel, C. A. C., de Sá, R. V., Schellevis, R. D., Waite, A. J., Blake, D. J., Veldink, J. H., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24453 · Cited by 268 · see citing works
Scotter, E. L., Vance, C. A., Nishimura, A. L., Lee, Y., Chen, H.-J., Urwin, H., Sardone, V., Mitchell, J. C., Rogelj, B., Rubinsztein, D. C., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.140087 · Cited by 265 · see citing works
Peters, O. M., Cabrera, G. T., Tran, H., Gendron, T. F., McKeon, J. E., Metterville, J., Weiss, A., Wightman, N., Salameh, J. S., Kim, J., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.018 · Cited by 259 · see citing works
Zhang, D., Iyer, L. M., He, F., & Aravind, L. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00283 · Cited by 244 · see citing works
Giannandrea, M., Bianchi, V., Mignogna, M. L., Sirri, A., Carrabino, S., D’Elia, E., Vecellio, M. L., Russo, S., Cogliati, F., Larizza, L., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.011 · Cited by 240 · see citing works
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 239 · see citing works
FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis
Hattula, K., & Peränen, J. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00864-2 · Cited by 233 · see citing works
Tao, Z., Wang, H., Qin, X., Li, K., Li, K., Jiang, X., Xu, G., Wang, G., & Ying, Z. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv005 · Cited by 233 · see citing works
Cady, J., Allred, P., Bali, T., Pestronk, A., Goate, A., Miller, T. M., Mitra, R. D., Ravits, J., Harms, M. B., & Baloh, R. H. (2014) · Annals of Neurology · doi:10.1002/ana.24306 · Cited by 220 · see citing works
Structure and function of the C-terminal PABC domain of human poly(A)-binding protein
Kozlov, G., Trempe, J., Khaleghpour, K., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071024998 · Cited by 205 · see citing works
Brady, O. A., Zheng, Y., Murphy, K. A., Huang, M. J., & Hu, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds475 · Cited by 205 · see citing works
TDP‐43 loss of function increases TFEB activity and blocks autophagosome–lysosome fusion
Xia, Q., Wang, H., Hao, Z., Fu, C., Hu, Q., Gao, F., Ren, H., Chen, D., Han, J., Ying, Z., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201591998 · Cited by 195 · cited 2× · see citing works
“Since TDP-43 regulates indirectly autophagy (Bose et al , 2011; Xia et al , 2016), we tested whether C9ORF72 or RAB39b can rescue autophagy misregulation caused by reduced expression of Tardbp .”
Discovery of a novel type of autophagy targeting RNA
Fujiwara, Y., Furuta, A., Kikuchi, H., Aizawa, S., Hatanaka, Y., Konya, C., Uchida, K., Yoshimura, A., Tamai, Y., Wada, K., et al. (2013) · Autophagy · doi:10.4161/auto.23002 · Cited by 186 · see citing works
Expanded ATXN2 CAG repeat size in ALS identifies genetic overlap between ALS and SCA2
Damme, P. V., Veldink, J. H., van Blitterswijk, M., Corveleyn, A., van Vught, P. W. J., Thijs, V., Dubois, B., Matthijs, G., van den Berg, L. H., & Robberecht, W. (2011) · Neurology · doi:10.1212/wnl.0b013e31821f445b · Cited by 177 · see citing works
Schaffer, B. E., Levin, R. S., Hertz, N. T., Maures, T. J., Schoof, M., Hollstein, P. E., Benayoun, B. A., Banko, M. R., Shaw, R. J., Shokat, K. M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.009 · Cited by 175 · see citing works
Ataxin-2 repeat-length variation and neurodegeneration
Ross, O. A., Rutherford, N. J., Baker, M., Soto‐Ortolaza, A. I., Carrasquillo, M. M., DeJesus-Hernandez, M., Adamson, J., Li, M., Volkening, K., Finger, E. C., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr227 · Cited by 172 · see citing works
Regulation of Autophagy by Neuropathological Protein TDP-43
Bose, J. K., Huang, C.-C., & Shen, C.-K. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237115 · Cited by 165 · see citing works
Incidence and extent of TDP-43 accumulation in aging human brain
Uchino, A., Takao, M., Hatsuta, H., Sumikura, H., Nakano, Y., Nogami, A., Saito, Y., Arai, T., Nishiyama, K., & Murayama, S. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0215-1 · Cited by 144 · see citing works
Yokoshi, M., Li, Q., Yamamoto, M., Okada, H., Suzuki, Y., & Kawahara, Y. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.022 · Cited by 139 · see citing works
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 · see citing works
Lattante, S., Ciura, S., Rouleau, G. A., & Kabashi, E. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.03.005 · Cited by 125 · see citing works
Self-citationvan Blitterswijk, M., Gendron, T. F., Baker, M., DeJesus‐Hernandez, M., Finch, N. A., Brown, P. H., Daughrity, L. M., Murray, M. E., Heckman, M. G., Jiang, J., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1480-6 · Cited by 123 · see citing works
Sato, T., Iwano, T., Kunii, M., Matsuda, S., Mizuguchi, R., Jung, Y., Hagiwara, H., Yoshihara, Y., Yuzaki, M., Harada, R., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.136903 · Cited by 123 · see citing works
Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP‐43
Urushitani, M., Sato, T., Bamba, H., Hisa, Y., & Tooyama, I. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22243 · Cited by 114 · see citing works
Taylor, J. P. (2015) · Neurology · doi:10.1212/wnl.0000000000001862 · Cited by 111 · see citing works
Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer
Nookala, R. K., Langemeyer, L., Pacitto, A., Ochoa-Montaño, B., Donaldson, J. C., Blaszczyk, B. K., Chirgadze, D. Y., Barr, F. A., Bazan, J. F., & Blundell, T. L. (2012) · Open Biology · doi:10.1098/rsob.120071 · Cited by 106 · see citing works
Association of Long ATXN2 CAG Repeat Sizes With Increased Risk of Amyotrophic Lateral Sclerosis
Daoud, H., Belzil, V., Martins, S., Sabbagh, M., Provencher, P., Lacomblez, L., Meininger, V., Camu, W., Dupré, N., Dion, P. A., et al. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.111 · Cited by 103 · see citing works
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 91 · see citing works
Lattante, S., de Calbiac, H., Le Ber, I., Brice, A., Ciura, S., & Kabashi, E. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu580 · Cited by 90 · cited 3× · see citing works
“At these concentrations, C9orf72 and mismatch AMOs do not lead to phenotypic features associated with deficient swimming or morphological abnormalities (Ciura et al , 2013; Lattante et al , 2015a,b).”
Self-citationContribution of ATXN2 intermediary polyQ expansions in a spectrum of neurodegenerative disorders
Lattante, S., Millecamps, S., Stévanin, G., Rivaud-Péchoux, S., Moigneu, C., Camuzat, A., da Barroca, S., Mundwiller, E., Couarch, P., Salachas, F., et al. (2014) · Neurology · doi:10.1212/wnl.0000000000000778 · Cited by 85 · see citing works
Self-citationRab8, POSH, and TAK1 regulate synaptic growth in a Drosophila model of frontotemporal dementia
West, R. J. H., Lu, Y., Marie, B., Gao, F., & Sweeney, S. T. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201404066 · Cited by 84 · see citing works
C9ORF72 repeat expansions in cases with previously identified pathogenic mutations
van Blitterswijk, M., Baker, M., DeJesus‐Hernandez, M., Ghidoni, R., Benussi, L., Finger, E. C., Hsiung, G. R., Kelley, B. J., Murray, M. E., Rutherford, N. J., et al. (2013) · Neurology · doi:10.1212/wnl.0b013e3182a8250c · Cited by 83 · see citing works
FLCN, a novel autophagy component, interacts with GABARAP and is regulated by ULK1 phosphorylation
Dunlop, E. A., Seifan, S., Claessens, T., Behrends, C., Kamps, M. A. F., Rozycka, E., Kemp, A. J., Nookala, R. K., Blenis, J., Coull, B. J., et al. (2014) · Autophagy · doi:10.4161/auto.29640 · Cited by 80 · see citing works
The mouse C9ORF72 ortholog is enriched in neurons known to degenerate in ALS and FTD
Suzuki, N., Maroof, A. M., Merkle, F. T., Koszka, K., Intoh, A., Armstrong, I. K. G., Moccia, R., Davis‐Dusenbery, B. N., & Eggan, K. C. (2013) · Nature Neuroscience · doi:10.1038/nn.3566 · Cited by 77 · see citing works
Xu, J., Fotouhi, M., & McPherson, P. S. (2015) · EMBO Reports · doi:10.15252/embr.201440006 · Cited by 59 · see citing works
Screening for C9ORF72 repeat expansion in FTLD
Ferrari, R., Mok, K. Y., Moreno, J. H., Cosentino, S., Goldman, J. S., Pietrini, P., Mayeux, R. P., Tierney, M. C., Kapogiannis, D., Jicha, G. A., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.017 · Cited by 53 · see citing works
Wilke, C., Pomper, J. K., Biskup, S., Puskás, C., Berg, D., & Synofzik, M. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8021-7 · Cited by 43 · see citing works
Seto, S., Sugaya, K., Tsujimura, K., Nagata, T., Horii, T., & Koide, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083324 · Cited by 41 · see citing works
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- Dunlop EA, Seifan S, Claessens T, Behrends C, Kamps MA, Rozycka E, Kemp AJ, Nookala RK, Blenis J, Coull BJ, Murray JT, van Steensel MA, Wilkinson S, ª 2016 The Authors The EMBO Journal Vol 35 | No 12 | 2016
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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 2,622 · see citing works
Self-citationAutophagy in major human diseases
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cadwell, K., Cecconi, F., Choi, A. M. K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108863 · Cited by 1,585 · see citing works
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · see citing works
The mammalian ULK1 complex and autophagy initiation
Zachari, M., & Ganley, I. G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170021 · Cited by 789 · see citing works
C9orf72-mediated ALS and FTD: multiple pathways to disease
Balendra, R., & Isaacs, A. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0047-2 · Cited by 715 · see citing works
Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons
Shi, Y., Lin, S., Staats, K. A., Li, Y., Chang, W.-H., Hung, S.-T., Hendricks, E., Linares, G. R., Wang, Y., Son, E. Y., et al. (2018) · Nature Medicine · doi:10.1038/nm.4490 · Cited by 566 · see citing works
The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy
Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404 · see citing works
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 · see citing works
Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works
Zhu, Q., Jiang, J., Gendron, T. F., McAlonis-Downes, M., Jiang, L., Taylor, A., Diaz Garcia, S., Ghosh Dastidar, S., Rodriguez, M. J., King, P., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0619-5 · Cited by 220 · see citing works
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238 · see citing works
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works
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 · see citing works
Self-citationLoss of C9orf72 Enhances Autophagic Activity via Deregulated mTOR and TFEB Signaling
Ugolino, J., Ji, Y. J., Conchina, K., Chu, J., Nirujogi, R. S., Pandey, A., Brady, N. R., Hamacher-Brady, A., & Wang, J. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1006443 · Cited by 185 · see citing works
Microglia and C9orf72 in neuroinflammation and ALS and frontotemporal dementia
Lall, D., & Baloh, R. H. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90607 · Cited by 175 · see citing works
Laflamme, C., McKeever, P. M., Kumar, R., Schwartz, J., Kolahdouzan, M., Chen, C. X., You, Z., Benaliouad, F., Gileadi, O., McBride, H. M., et al. (2019) · eLife · doi:10.7554/elife.48363 · Cited by 155 · see citing works
Boivin, M., Pfister, V., Gaucherot, A., Ruffenach, F., Negroni, L., Sellier, C., & Charlet‐Berguerand, N. (2020) · The EMBO Journal · doi:10.15252/embj.2018100574 · Cited by 137 · see citing works
Self-citationBéland, L.-C., Markovinovic, A., Jakovac, H., De Marchi, F., Bilic, E., Mazzini, L., Kriz, J., & Munitic, I. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa124 · Cited by 125 · see citing works
Lehmer, C., Oeckl, P., Weishaupt, J. H., Volk, A. E., Diehl‐Schmid, J., Schroeter, M. L., Lauer, M., Kornhuber, J., Levin, J., Fassbender, K., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607486 · Cited by 118 · see citing works
Synaptic dysfunction and altered excitability in C9ORF72 ALS/FTD
Starr, A., & Sattler, R. (2018) · Brain Research · doi:10.1016/j.brainres.2018.02.011 · Cited by 78 · see citing works
Campanari, M.-L., García-Ayllón, M.-S., Ciura, S., Sáez-Valero, J., & Kabashi, E. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00160 · Cited by 69 · see citing works
Self-citationRecent progress in the role of autophagy in neurological diseases
Meng, T., Lin, S., Zhuang, H., Huang, H., He, Z., Hu, Y., Gong, Q., & Feng, D. (2019) · Cell Stress · doi:10.15698/cst2019.05.186 · Cited by 58 · see citing works
WDR41 supports lysosomal response to changes in amino acid availability
Amick, J., Tharkeshwar, A. K., Amaya, & Ferguson, S. M. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-12-0703 · Cited by 39 · see citing works
Could sirtuin activities modify ALS onset and progression?
Tang, B. L. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0452-2 · Cited by 24 · see citing works
Lost & found: C9ORF72 and the autophagy pathway in ALS/FTD
Almeida, S., & Gao, F. (2016) · The EMBO Journal · doi:10.15252/embj.201694578 · Cited by 13 · see citing works
- Authors
- Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., & Charlet‐Berguerand, N.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Sellier, Chantal
- Charlet‐Berguerand, Nicolas
- ORCID
- Venue
- The EMBO Journal
- Published
- 2016-04-21
- Volume
- 35
- Issue
- 12
- Pages
- 1276-1297
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC4910533
- OpenAlex
- W2336528486
- Cited by
- 414
- References
- 122
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 33 · 2023: 30 · 2022: 31 · 2021: 72 · 2020: 53 · 2019: 45 · 2018: 47 · 2017: 42 · 2016: 20
- FWCI
- 38.60
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Fondation de France Thierry Latran (#57486)
- ATIP‐Avenir INSERM
- Robert Packard Foundation
- E‐rare ERA‐NET program
- AFM (#18605)
- ARSLA
- France‐Alzheimer Association (C9orfish)
- Investissements d'avenir (ANR‐10‐IAIHU‐06)
- Fondation Cognacq‐Jay
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- C9orf72, ATXN2, polyglutamine expansion, amyotrophic lateral sclerosis, frontotemporal dementia, autophagy, autophagic flux, Rab8a, RAB39B, SMCR8, TBK1, TDP-43 aggregation, motor neuron dysfunction, neuronal cell death, GGGGCC repeat expansion
- MeSH terms
- Ataxin-2, C9orf72 Protein, Amyotrophic Lateral Sclerosis, Autophagy, Humans, Motor Neurons, Peptides, Proteins, Cell Death, Frontotemporal Dementia
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 ›
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