Corrigendum: Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
Luke McAlary
Steven S. Plotkin
Justin J. Yerbury
Neil R. Cashman- 1Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia
- 2Molecular Horizons and School of Chemistry and Molecular Bioscience, Faculty of Science, Medicine and Health, University of Wollongong, Wollongong, NSW, Australia
- 3Department of Physics and Astronomy, University of British Columbia, Vancouver, BC, Canada
- 4Genome Sciences and Technology Program, University of British Columbia, Vancouver, BC, Canada
- 5Djavad Mowafaghian Centre for Brain Health, University of British Columbia, Vancouver, BC, Canada
A Corrigendum on
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
by McAlary, L., Plotkin, S. S., Yerbury, J. J., and Cashman, N. R. (2019). Front. Mol. Neurosci. 12:262. doi: 10.3389/fnmol.2019.00262
In the original article, there was a mistake in Table 1 as published. The incorrect original research articles were referenced for some of the table cells. The corrected Table 1 appears below.
Table 1. Evidence supporting the prion-like characteristics of ALS-associated proteins.
The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.
References
Ayers, J. I., Diamond, J., Sari, A., Fromholt, S., Galaleldeen, A., Ostrow, L. W., et al. (2016a). Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS. Acta Neuropathol. 132, 827–840. doi: 10.1007/s00401-016-1623-4
Ayers, J. I., Fromholt, S., Koch, M., DeBosier, A., McMahon, B., Xu, G., et al. (2014). Experimental transmissibility of mutant SOD1 motor neuron disease. Acta Neuropathol. 128, 791–803. doi: 10.1007/s00401-014-1342-7
Chattopadhyay, M., Durazo, A., Sohn, S. H., Strong, C. D., Gralla, E. B., Whitelegge, J. P., et al. (2008). Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc. Natl. Acad. Sci. U S A. 105, 18663–18668. doi: 10.1073/pnas.0807058105
Chia, R., Tattum, M. H., Jones, S., Collinge, J., Fisher, E. M. C., and Jackson, G. S. (2010). Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis. PLoS ONE 5:e10627. doi: 10.1371/journal.pone.0010627
Ekhtiari Bidhendi, E., Bergh, J., Zetterström, P., Forsberg, K., Pakkenberg, B., Andersen, P. M., et al. (2018). Mutant superoxide dismutase aggregates from human spinal cord transmit amyotrophic lateral sclerosis. Acta Neuropathol. 136, 939–953. doi: 10.1007/s00401-018-1915-y
Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K., and Nukina, N. (2011). A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. J. Biol. Chem. 286, 18664–18672. doi: 10.1074/jbc.M111.231209
Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O'Neill, M. A., et al. (2014). Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Proc. Natl. Acad. Sci. U.S.A. 111, 3620–3625. doi: 10.1073/pnas.1312245111
Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., and Gitler, A. D. (2009). TDP-43 is intrinsically aggregation-prone and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284, 20329–20339. doi: 10.1074/jbc.M109.010264
Munch, C., O'Brien, J., and Bertolotti, A. (2011). Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 108, 3548–3553. doi: 10.1073/pnas.1017275108
Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N., and Furukawa, Y. (2014). Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. J. Biol. Chem. 289, 1192–1202. doi: 10.1074/jbc.M113.516492
Nonaka, T., Masuda-Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., et al. (2013). Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep. 4, 124–134. doi: 10.1016/j.celrep.2013.06.007
Pokrishevsky, E., Hong, R. H., Mackenzie, I. R., and Cashman, N. R. (2017). Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells. PLOS ONE 12:e0184384. doi: 10.1371/journal.pone.0184384
Porta, S., Xu, Y., Restrepo, C. R., Kwong, L. K., Zhang, B., Brown, H. J., et al. (2018). Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo. Nat. Commun. 9:4220. doi: 10.1038/s41467-018-06548-9
Keywords: amyotrophic lateral sclerosis, protein misfolding, protein aggregation, prion, proteostasis
Citation: McAlary L, Plotkin SS, Yerbury JJ and Cashman NR (2020) Corrigendum: Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis. Front. Mol. Neurosci. 12:311. doi: 10.3389/fnmol.2019.00311
Received: 09 November 2019; Accepted: 04 December 2019;
Published: 21 January 2020.
Edited and reviewed by: Tiago F. Outeiro, University Medical Center Goettingen, Germany
Copyright © 2020 McAlary, Plotkin, Yerbury and Cashman. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Neil R. Cashman, neil.cashman@vch.ca