This article is a correction to:
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François-Moutal1,2
Samantha Perez-Miller1,2
David D. Scott1,2
Victor G. Miranda1,2
Niloufar Mollasalehi1,2,3
May Khanna1,2*- 1Department of Pharmacology, College of Medicine, University of Arizona, Tucson, AZ, United States
- 2Center for Innovation in Brain Science, Tucson, AZ, United States
- 3Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, United States
A Corrigendum on
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
by François-Moutal, L., Perez-Miller, S., Scott, D. D., Miranda, V. G., Mollasalehi, N., and Khanna, M. (2019). Front. Mol. Neurosci. 12:301. doi: 10.3389/fnmol.2019.00301
In the original article, there was an error. In “Binding of Zinc was shown to increase TDP-43 thermostability and formed Thioflavin-T-positive aggregates, reminiscent of amyloid nuclei (Garnier et al., 2017).” The word “increase” should be replaced by “decrease”.
A correction has been made to the Introduction section, subsection Post-translational Modifications of TDP-43, sub-subsection Zinc Binding, paragraph 1:
“A recent study described the ability of zinc ions to bind TDP-43 with an affinity in the micromolar range. Binding of Zinc was shown to decrease TDP-43 thermostability and formed Thioflavin-T-positive aggregates, reminiscent of amyloid nuclei (Garnier et al., 2017). Zinc treated SY5Y neuronal-like cells recapitulated several hallmarks of TDP-43 proteinopathy including reduced expression, formation of small nuclear inclusions, and diffuse cytosolic localization. The treatment, however, did not cause formation of CTD fragments, ubiquitination or phosphorylation of TDP-43 (Caragounis et al., 2010). Although an indirect route was not ruled out, especially via the generation of ROS through NMDA- or mitochondrial-mediated pathways by Zn2+, zinc ions are also known to bind and promote in vitro aggregation of Tau (Huang et al., 2014), alpha-synuclein (αSyn) (Valiente-Gabioud et al., 2012) and Amyloid-β Peptide(Aβ) (Alies et al., 2016). Altered zinc homeostasis is also suggested as a risk factor for several neurodegenerative disorders such as ALS or Alzheimer's disease [see review (Szewczyk, 2013)]. Even though this is still a matter of debate given the relatively poor affinity of zinc for those proteins (in the micromolar range), direct contribution of zinc to TDP-43 aggregation could lead to complexes actively producing ROS similar to Aβ and αSyn (Atrián-Blasco et al., 2018), and further amplifying toxicity.”
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
Alies, B., Conte-Daban, A., Sayen, S., Collin, F., Kieffer, I., Guillon, E., et al. (2016). Zinc(II) binding site to the Amyloid-β peptide: insights from spectroscopic studies with a wide series of modified peptides. Inorg. Chem. 55, 10499–10509. doi: 10.1021/acs.inorgchem.6b01733
Atrián-Blasco, E., Gonzalez, P., Santoro, A., Alies, B., Faller, P., and Hureau, C. (2018). Cu and Zn coordination to amyloid peptides: from fascinating chemistry to debated pathological relevance. Coord. Chem. Rev. 371, 38–55. doi: 10.1016/j.ccr.2018.04.007
Caragounis, A., Price, K. A., Soon, C. P. W., Filiz, G., Masters, C. L., Li, Q. X., et al. (2010). Zinc induces depletion and aggregation of endogenous TDP-43. Free Radic. Biol. Med. 48, 1152–1161. doi: 10.1016/j.freeradbiomed.2010.01.035
Garnier, C., Devred, F., Byrne, D., Puppo, R., Roman, A. Y., Malesinski, S., et al. (2017). Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates. Sci. Rep. 7:6812. doi: 10.1038/s41598-017-07215-7
Huang, Y., Wu, Z., Cao, Y., Lang, M., Lu, B., and Zhou, B. (2014). Zinc binding directly regulates tau toxicity independent of tau hyperphosphorylation. Cell Rep. 8, 831–842. doi: 10.1016/j.celrep.2014.06.047
Valiente-Gabioud, A. A., Torres-Monserrat, V., Molina-Rubino, L., Binolfi, A., Griesinger, C., and Fernández, C. O. (2012). Structural basis behind the interaction of Zn2 + with the protein α-synuclein and the Aβ peptide: a comparative analysis. J. Inorg. Biochem. 117, 334–341. doi: 10.1016/j.jinorgbio.2012.06.011
Keywords: TDP-43 = TAR DNA–binding protein 43, structure, post-translational modification, subdomains, RRM domain
Citation: François-Moutal L, Perez-Miller S, Scott DD, Miranda VG, Mollasalehi N and Khanna M (2020) Corrigendum: Structural Insights Into TDP-43 and Effects of Post-translational Modifications. Front. Mol. Neurosci. 13:45. doi: 10.3389/fnmol.2020.00045
Received: 06 February 2020; Accepted: 06 March 2020;
Published: 02 April 2020.
Edited and reviewed by: Serena Carra, University of Modena and Reggio Emilia, Italy
Copyright © 2020 François-Moutal, Perez-Miller, Scott, Miranda, Mollasalehi and Khanna. 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: May Khanna, bWF5a2hhbm5hJiN4MDAwNDA7ZW1haWwuYXJpem9uYS5lZHU=