ALS/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function
Open accessAbstract
Significance: Mutations in UBQLN2 cause amyotrophic lateral sclerosis with frontotemporal dementia (ALS/FTD). UBQLN2 regulates proteostasis by clearing misfolded proteins from cells through the proteasome and autophagy degradation pathways. Here, we report on defects in autophagy that results from knockout or expression of WT and ALS/FTD mutant UBQLN2 proteins in cells and mice. We show that loss of UBQLN2 reduces expression of ATP6v1g1, a critical subunit of the ATPase pump that regulates vacuolar acidification and is required for the maturation of autophagosomes. We show that WT but not ALS/FTD mutant UBQLN2 proteins can rescue the acidification defect. Furthermore, WT but not ALS/FTD mutant UBQLN2 proteins bind and stimulate ATP6v1g1 biogenesis, suggesting an important role played by UBQLN2 in V-ATPase regulation.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
UBQLN2 modulates MTORC1 activity, lysosomal acidification, and autophagosome maturation.
“UBQLN2 modulates MTORC1 activity, lysosomal acidification, and, in turn, autophagosome maturation [229–231].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [230]
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Guide for the Care and Use of Laboratory Animals: Eighth Edition
(2011) · doi:10.17226/12910 · Cited by 16,199 · see citing works
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,467 · see citing works
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214 · see citing works
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,153 · see citing works
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 · see citing works
Autophagy: cellular and molecular mechanisms
Glick, D. R., Barth, S., & Macleod, K. F. (2010) · The Journal of Pathology · doi:10.1002/path.2697 · Cited by 3,814 · see citing works
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 · see citing works
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124 · see citing works
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472 · see citing works
Yoshimori, T., Yamamoto, A., Moriyama, Y., Futai, M., & Tashiro, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47429-2 · Cited by 1,334 · see citing works
Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.05.008 · Cited by 1,212 · 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
Self-citationMonitoring and Measuring Autophagy
Yoshii, S. R., & Mizushima, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091865 · Cited by 1,107 · see citing works
Methods for monitoring autophagy
Mizushima, N. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.005 · Cited by 884 · see citing works
Polson, H. E. J., de Lartigue, J., Rigden, D. J., Reedijk, M., Urbé, S., Clague, M. J., & Tooze, S. A. (2010) · Autophagy · doi:10.4161/auto.6.4.11863 · Cited by 712 · see citing works
The hPLIC Proteins May Provide a Link between the Ubiquitination Machinery and the Proteasome
Kleijnen, M. F., Shih, A. H., Zhou, P., Kumar, S., Soccio, R. E., Kedersha, N., Gill, G., & Howley, P. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00040-x · Cited by 352 · see citing works
PLIC proteins or ubiquilins regulate autophagy‐dependent cell survival during nutrient starvation
N'Diaye, E., Kajihara, K. K., Hsieh, I., Morisaki, H., Debnath, J., & Brown, E. J. (2009) · The EMBO Reports · doi:10.1038/embor.2008.238 · Cited by 323 · see citing works
Dao, T. P., Kolaitis, R.-M., Kim, H.-J., O'Donovan, K., Martyniak, B., Colicino, E., Hehnly, H., Taylor, J. P., & Castañeda, C. A. (2018) · Molecules and Cells · doi:10.1016/j.molcel.2018.02.004 · Cited by 319 · see citing works
UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome
Hjerpe, R., Bett, J. S., Keuss, M. J., Solovyova, A. S., McWilliams, T. G., Johnson, C., Sahu, I., Varghese, J., Wood, N. T., Wightman, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.001 · Cited by 310 · see citing works
ALS Genes in the Genomic Era and their Implications for FTD
Nguyen, H. P., Broeckhoven, C. V., & van der Zee, J. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.03.001 · Cited by 308 · see citing works
Bimolecular Fluorescence Complementation (BiFC): A 5-year Update and Future Perspectives
Kodama, Y., & Hu, C. (2012) · BioTechniques · doi:10.2144/000113943 · Cited by 287 · see citing works
Lysosome trafficking and signaling in health and neurodegenerative diseases
Lie, P. P. Y., & Nixon, R. A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.015 · Cited by 269 · see citing works
Ubiquilins Chaperone and Triage Mitochondrial Membrane Proteins for Degradation
Itakura, E., Zavodszky, E., Shao, S., Wohlever, M. L., Keenan, R. J., & Hegde, R. S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.020 · Cited by 255 · see citing works
The vacuolar-type H+-ATPase at a glance – more than a proton pump
Maxson, M. E., & Grinstein, S. (2014) · Journal of Cell Science · doi:10.1242/jcs.158550 · Cited by 234 · see citing works
Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
Rothenberg, C., Srinivasan, D., Mah, L., Kaushik, S., Peterhoff, C. M., Ugolino, J., Fang, S., Cuervo, A. M., Nixon, R. A., & Monteiro, M. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq231 · Cited by 225 · see citing works
Self-citationSautin, Y. Y., Lu, M., Gaugler, A. C., Zhang, L., & Gluck, S. L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.575-589.2005 · Cited by 212 · see citing works
An Improved Bimolecular Fluorescence Complementation Assay with a High Signal-To-Noise Ratio
Kodama, Y., & Hu, C. (2010) · BioTechniques · doi:10.2144/000113519 · Cited by 206 · see citing works
Mah, A. L., Perry, G. L., Smith, M. A., & Monteiro, M. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.4.847 · Cited by 203 · see citing works
Self-citationEukaryotic V-ATPase: Novel structural findings and functional insights
Marshansky, V. N., Rubinstein, J. L., & Grüber, G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.01.018 · Cited by 196 · see citing works
Götzl, J. K., Mori, K., Daμμe, M., Fellerer, K., Tahirović, S., Kleinberger, G., Janssens, J., van der Zee, J., Lang, C. M., Kremmer, E., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1262-6 · Cited by 195 · see citing works
Rudnick, N. D., Griffey, C. J., Guarnieri, P., Gerbino, V., Wang, X., Piersaint, J. A., Tapia, J. C., Rich, M. M., & Maniatis, T. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704294114 · Cited by 189 · see citing works
SQSTM1/p62: a potential target for neurodegenerative disease
Ma, S., Attarwala, I. Y., & Xie, X.-Q. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00516 · Cited by 185 · see citing works
Ko, H. S., Uehara, T., Tsuruma, K., & Nomura, Y. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.04.031 · Cited by 184 · see citing works
Brettschneider, J., Deerlin, V. M. V., Robinson, J. L., Kwong, L. K., Lee, E. B., Ali, Y., Safren, N., Monteiro, M. J., Toledo, J. B., Elman, L. B., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0970-z · Cited by 183 · see citing works
Self-citationUBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis
Williams, K. L., Warraich, S. T., Yang, S., Fifita, J. A., Fernando, R., Rouleau, G. A., Nicholson, G. A., & Blair, I. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.008 · Cited by 166 · see citing works
Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)
Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · cited 1× · see citing works
“The impairment in autophagosome acidification found in our studies is also noteworthy, as it adds to growing evidence of similar defects in acidification that have been found within the endosomal–lysosomal system of several neurodegenerative diseases, including Alzheimer’s disease and Down syndrome (53, 70, 71).”
ResultAutophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand
Ramesh, N., & Pandey, U. B. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00263 · Cited by 150 · see citing works
Wu, A. L., Wang, J., Zheleznyak, A., & Brown, E. J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80212-9 · Cited by 140 · see citing works
New insights into the regulation of V-ATPase-dependent proton secretion
Breton, S., & Brown, D. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00340.2006 · Cited by 138 · see citing works
Ubiquilin 2 modulates ALS/FTD-linked FUS–RNA complex dynamics and stress granule formation
Alexander, E. J., Niaki, A. G., Zhang, T., Sarkar, J., Liu, Y., Nirujogi, R. S., Pandey, A., Myong, S., & Wang, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1811997115 · Cited by 128 · see citing works
Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification
Şentürk, M., Lin, G., Zuo, Z., Mao, D., Watson, E., Mikos, A. G., & Bellen, H. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0281-x · Cited by 124 · see citing works
V1-situated Stalk Subunits of the Yeast Vacuolar Proton-translocating ATPase
Tomashek, J. J., Graham, L. A., Hutchins, M. U., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26787 · Cited by 97 · see citing works
Overexpression of ubiquilin decreases ubiquitination and degradation of presenilin proteins
Massey, L. K., Mah, A. L., Ford, D. L., Miller, J. L., Liang, J., Doong, H., & Monteiro, M. J. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6109 · Cited by 93 · see citing works
Self-citationUbiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein*
Stieren, E. S., Ayadi, A. E., Xiao, Y., Siller, E., Landsverk, M., Oberhauser, A., Barral, J., & Boehning, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243147 · Cited by 93 · see citing works
Le, N. T. T., Chang, L., Kovlyagina, I., Georgiou, P., Safren, N., Braunstein, K. E., Kvarta, M. D., Dyke, A. M. V., LeGates, T. A., Philips, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608432113 · Cited by 89 · see citing works
Self-citationA family of ubiquitin‐like proteins binds the ATPase domain of Hsp70‐like Stch
Kaye, F. J., Modi, S., Ivanovska, I. L., Koonin, E. V., Thress, K. S., Kubo, A., Kornbluth, S. A., & Rose, M. D. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01135-2 · Cited by 89 · see citing works
Dao, T. P., Martyniak, B., Canning, A. J., Lei, Y., Colicino, E. G., Cosgrove, M. S., Hehnly, H., & Castañeda, C. A. (2019) · Structure · doi:10.1016/j.str.2019.03.012 · Cited by 87 · see citing works
Ling, S., Dastidar, S. G., Tokunaga, S., Ho, W. Y., Lim, K., Ilieva, H. S., Parone, P. A., Tyan, S.-H., Tse, T. M., Chang, J., et al. (2019) · eLife · doi:10.7554/elife.40811 · Cited by 85 · see citing works
Self-citationUbiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery
Lee, D. Y., Arnott, D. P., & Brown, E. J. (2013) · EMBO Reports · doi:10.1038/embor.2013.22 · Cited by 78 · see citing works
Chang, L., & Monteiro, M. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130162 · Cited by 77 · see citing works
Self-citationDendritic spinopathy in transgenic mice expressing ALS/dementia-linked mutant UBQLN2
Gorrie, G., Fecto, F., Radzicki, D., Weiss, C., Shi, Y., Dong, H., Zhai, H., Fu, R., Liu, E., Li, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405741111 · Cited by 76 · see citing works
Self-citationPathogenic Ubqln2 gains toxic properties to induce neuron death
Wu, Q., Liu, M., Huang, C., Liu, X., Huang, B., Li, N., Zhou, H., & Xia, X. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1367-y · Cited by 75 · see citing works
Ohira, M., Smardon, A. M., Charsky, C. M. H., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601441200 · Cited by 72 · see citing works
The Rab-interacting lysosomal protein (RILP) regulates vacuolar ATPase acting on the V1G1 subunit
Luca, M. D., Cogli, L., Progida, C., Nisi, V., Pascolutti, R., Sigismund, S., Fiore, P. P. D., & Bucci, C. (2014) · Journal of Cell Science · doi:10.1242/jcs.142604 · Cited by 69 · see citing works
Xia, Y., Yan, L. H., Huang, B., Liu, M., Liu, X., & Huang, C. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12606 · Cited by 65 · see citing works
Kurlawala, Z., Shah, P. P., Shah, C., et al. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25880 · Cited by 59 · see citing works
Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia Continuum
Shahheydari, H., Ragagnin, A., Walker, A. K., Toth, R. P., Vidal, M., Jagaraj, C. J., Perri, E. R., Konopka, A., Sultana, J. M., & Atkin, J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00119 · Cited by 59 · see citing works
ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1
Gilpin, K. M., Chang, L., & Monteiro, M. J. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv020 · Cited by 58 · see citing works
Self-citationGavriilidis, C., Laredj, L., Solinhac, R., Messaddeq, N., Viaud, J., Laporte, J., Sumara, I., & Hnia, K. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0024-9 · Cited by 56 · see citing works
Mutant UBQLN2 promotes toxicity by modulating intrinsic self-assembly
Sharkey, L. M., Safren, N., Pithadia, A. S., Gerson, J. E., Dulchavsky, M. E., Fischer, S., Patel, R., Lantis, G., Ashraf, N., Kim, J. H., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810522115 · Cited by 52 · see citing works
Conklin, D., Holderman, S. D., Whitmore, T. E., Maurer, M. F., & Feldhaus, A. L. (2000) · Gene · doi:10.1016/s0378-1119(00)00122-0 · Cited by 48 · see citing works
A novel ALS-associated variant in UBQLN4 regulates motor axon morphogenesis
Edens, B. M., Yan, J., Miller, N., Deng, H., Siddique, T., & Ma, Y. C. (2017) · eLife · doi:10.7554/elife.25453 · Cited by 48 · see citing works
Self-citationWhiteley, A. M., Prado, M. A., Peng, I., Abbas, A. R., Haley, B., Paulo, J. A., Reichelt, M., Katakam, A. K., Sagolla, M. S., Modrusan, Z. D., et al. (2017) · eLife · doi:10.7554/elife.26435 · Cited by 48 · see citing works
Self-citationChen, X., Ebelle, D. L., Wright, B. J., Sridharan, V., Hooper, E., & Walters, K. J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.01.021 · Cited by 47 · see citing works
Ford, D. L., & Monteiro, M. J. (2006) · Biochemical Journal · doi:10.1042/bj20060441 · Cited by 39 · see citing works
Self-citationRILP regulates vacuolar ATPase through interaction with the V1G1 subunit
Luca, M. D., Cogli, L., Progida, C., et al. (2015) · Journal of Cell Science · doi:10.1242/jcs.175323 · Cited by 39 · see citing works
The Ubiquitin-like Protein PLIC-2 Is a Negative Regulator of G Protein-coupled Receptor Endocytosis
N’Diaye, E.-N., Hanyaloglu, A. C., Kajihara, K. K., Puthenveedu, M. A., Wu, P., von Zastrow, M., & Brown, E. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0775 · Cited by 36 · see citing works
Protein recycling pathways in neurodegenerative diseases
Fecto, F., Esengul, Y. T., & Siddique, T. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt243 · Cited by 33 · see citing works
Self-citationGkazi, S. A., Troakes, C., Topp, S. D., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.08.015 · Cited by 22 · see citing works
Scotter, E. L., Smyth, L. C. D., Bailey, J. W. T., Wong, C. H., de Majo, M., Vance, C. A., Synek, B. J. L., Turner, C. P., Pereira, J. A., Charleston, A. J., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.06.019 · Cited by 21 · see citing works
Self-citationMatsuda, M., Koide, T., Yorihuzi, T., et al. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4149 · Cited by 20 · see citing works
Lou Gehrig’s Disease (ALS): UBQLN2 Mutations Strike Out of Phase
Higgins, N., Lin, B., & Monteiro, M. J. (2019) · Structure · doi:10.1016/j.str.2019.05.006 · Cited by 20 · see citing works
Self-citationThe specificity of ubiquitin binding to ubiquilin-1 is regulated by sequences besides its UBA domain
Harman, C. A., & Monteiro, M. J. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.06.002 · Cited by 20 · see citing works
Self-citationSignature changes in ubiquilin expression in the R6/2 mouse model of Huntington’s disease
Safren, N., Chang, L., Dziki, K. M., & Monteiro, M. J. (2014) · Brain Research · doi:10.1016/j.brainres.2014.12.008 · Cited by 16 · see citing works
Self-citationUgolino, J., Dziki, K. M., Kim, A., Wu, J. J., Vogel, B. E., & Monteiro, M. J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220849 · Cited by 10 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
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-citationMead, R. J., Shan, N., Reiser, H. J., Marshall, F., & Shaw, P. J. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00612-2 · Cited by 505 · see citing works
Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases
Nixon, R. A., & Rubinsztein, D. C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00757-5 · Cited by 435 · 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
The Cytotoxicity and Clearance of Mutant Huntingtin and Other Misfolded Proteins
Folger, A., & Wang, Y. (2021) · Cells · doi:10.3390/cells10112835 · Cited by 32 · see citing works
- Authors
- Wu, J. J., Cai, A., Greenslade, J. E., Higgins, N. R., Fan, C., Le, N. T. T., Tatman, M., Whiteley, A. M., Prado, M. A., Dieriks, B. V., Curtis, M. A., Shaw, C. E., Siddique, T., Faull, R. L. M., Scotter, E. L., Finley, D., & Monteiro, M. J.
- Affiliations
- University of Maryland, Baltimore (US)
- Harvard University (US)
- University of Auckland (NZ)
- King's College London (GB)
- Northwestern University (US)
- Corresponding author
- Monteiro, Mervyn J.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2020-06-08
- Volume
- 117
- Issue
- 26
- Pages
- 15230-15241
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC7334651
- OpenAlex
- W3033186313
- Cited by
- 86
- References
- 76
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 15 · 2023: 17 · 2022: 15 · 2021: 12 · 2020: 8
- FWCI
- 9.32
- Type
- journal article
- Language
- en
- Update notices
- correction (2021-08-30)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- ResearchSpace (University of Auckland) (submittedVersion)
- Funders
- HHS | NIH | National Institute of Neurological Disorders and Stroke (R01NS098243, R01NS100008, R01NS078504, R01NS046535)
- The Robert Packard Center for ALS Research at Johns Hopkins (17-IIP-356-1)
- The ALS Association (17-IIP-356-1)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- UBQLN2, amyotrophic lateral sclerosis, frontotemporal dementia, autophagy, V-ATPase, proteostasis, protein misfolding, loss-of-function mutations, autophagosome maturation, proteasome
- MeSH terms
- Autophagosomes, Autophagy-Related Proteins, Sequestosome-1 Protein, Amyotrophic Lateral Sclerosis, Animals, Autophagy, Cell Line, Dementia, Humans, Hydrogen-Ion Concentration, Mice, Transgenic, Microtubule-Associated Proteins, Mutation, Protein Binding, Biomarkers, Up-Regulation, Genetic Predisposition to Disease, Vacuolar Proton-Translocating ATPases, Adaptor Proteins, Signal Transducing, Mice, Lysosomal Membrane Proteins, Lysosomal-Associated Membrane Protein 1
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