Literature DB >> 32300293

Corrigendum: 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.   

Abstract

[This corrects the article DOI: 10.3389/fnmol.2019.00301.].
Copyright © 2020 François-Moutal, Perez-Miller, Scott, Miranda, Mollasalehi and Khanna.

Entities:  

Keywords:  RRM domain; TDP-43 = TAR DNA–binding protein 43; post-translational modification; structure; subdomains

Year:  2020        PMID: 32300293      PMCID: PMC7143466          DOI: 10.3389/fnmol.2020.00045

Source DB:  PubMed          Journal:  Front Mol Neurosci        ISSN: 1662-5099            Impact factor:   5.639


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.
  7 in total

1.  Zinc induces depletion and aggregation of endogenous TDP-43.

Authors:  Aphrodite Caragounis; Katherine Ann Price; Cynthia P W Soon; Gulay Filiz; Colin L Masters; Qiao-Xin Li; Peter J Crouch; Anthony R White
Journal:  Free Radic Biol Med       Date:  2010-02-04       Impact factor: 7.376

2.  Structural basis behind the interaction of Zn²⁺ with the protein α-synuclein and the Aβ peptide: a comparative analysis.

Authors:  Ariel A Valiente-Gabioud; Valentina Torres-Monserrat; Laura Molina-Rubino; Andres Binolfi; Christian Griesinger; Claudio O Fernández
Journal:  J Inorg Biochem       Date:  2012-06-29       Impact factor: 4.155

3.  Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.

Authors:  Elena Atrián-Blasco; Paulina Gonzalez; Alice Santoro; Bruno Alies; Peter Faller; Christelle Hureau
Journal:  Coord Chem Rev       Date:  2018-09-15       Impact factor: 22.315

4.  Zinc binding directly regulates tau toxicity independent of tau hyperphosphorylation.

Authors:  Yunpeng Huang; Zhihao Wu; Yu Cao; Minglin Lang; Bingwei Lu; Bing Zhou
Journal:  Cell Rep       Date:  2014-07-24       Impact factor: 9.423

5.  Zinc homeostasis and neurodegenerative disorders.

Authors:  Bernadeta Szewczyk
Journal:  Front Aging Neurosci       Date:  2013-07-19       Impact factor: 5.750

6.  Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.

Authors:  Cyrille Garnier; François Devred; Deborah Byrne; Rémy Puppo; Andrei Yu Roman; Soazig Malesinski; Andrey V Golovin; Régine Lebrun; Natalia N Ninkina; Philipp O Tsvetkov
Journal:  Sci Rep       Date:  2017-07-28       Impact factor: 4.379

7.  Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides.

Authors:  Bruno Alies; Amandine Conte-Daban; Stéphanie Sayen; Fabrice Collin; Isabelle Kieffer; Emmanuel Guillon; Peter Faller; Christelle Hureau
Journal:  Inorg Chem       Date:  2016-09-26       Impact factor: 5.165

  7 in total

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