Journal Article (Erratum/Correction)

DZNE-2026-00773

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Correction: A rare missense variant impacting NEK1 kinase function is associated with ALS.

Brenner, D. (First author)DZNE* ; Ponomarenko, A. ; Petrut, I. ; Beyrle, S. ; Contardo, M. ; Loss, I. ; Radke, C. ; Frank, J. ; Zimmer, E. ; Schlesner, M. ; Achenbach, P. ; Scheveneels, W. ; Aly, A. ; Nazlican, H. ; Hesebeck-Brinkmann, J. ; Oeckl, P.DZNE* ; Müller, K. ; Siebert, R. ; Böckers, T.DZNE* ; van Eijk, K. ; Veldink, J. ; Kleger, A. ; Mulaw, M. ; Andersen, P. M. ; Forsberg, K. ; Weishaupt, J. H.DZNE* ; Loghmani, S. B. ; Grehl, T. ; van Damme, P. ; Weis, J. ; Catanese, A. (Last author)DZNE*

2026
Biomed Central London

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Please use a persistent id in citations: doi:10.1186/s40478-026-02380-1

Abstract: Correction: Acta Neuropathol Commun 14, 135 (2026)https://doi.org/10.1186/s40478-026-02351-6In this article [1], the figure citations for Figs. 4 and 5, and 6 in the paragraph “Notably, while NEK1 kinase activity has been proposed. translocation in control MNs” were incorrect.Notably, while NEK1 kinase activity has been proposed as the principal pathomechanism in NEK1-ALS [8], this hypothesis still required in vivo confirmation. NEK1 p.N598S MN cultures exhibited increased susceptibility to DNA damage and ciliary abnormalities (Fig. 4C-G), both processes known to depend on NEK1 kinase func­tion [9, 15]. This led us to hypothesize that the p.N598S variant might directly impact NEK1 kinase activity. To test this, we quantified the phosphorylation of the estab­lished direct NEK1 target YAP1 at tyrosine 407 (pTyr407) [16]. Both p.N598S- and p.R812*-mutant MN cultures showed reduced YAP1 pTyr407 levels compared with their isogenic counterpart (Fig. 5A), supporting reduced kinase activity. This was further assessed in whole lysates from MN cultures, and in immunopurified NEK1-WT and p.N598S. Overall kinase activity was markedly reduced in both p.N598S- and p.R812*-mutant cultures compared to wild-type MNs (Fig. 5B). Direct measure­ment of purified NEK1 confirmed that the p.N598S vari­ant displayed reduced kinase activity compared with wild-type NEK1 (Fig. 5C).To further establish causality, we treated MNs derived from three healthy donors with the NEK1-specific inhibi­tor BSc5367. Exposure to 11.5 nM BSc5367 for 48 h sig­nificantly reduced kinase activity (Fig. 6A), decreased YAP1 phosphorylation at Tyr407 (Fig. 6B), and increased γH2A.X levels (Fig. 6C). Most notably, pharmacological inhibition of NEK1 was also sufficient to induce TDP- 43 nucleocytoplasmic translocation in control MNs (Fig. 6D).These citations have now been corrected in the original publication.The original article has been corrected.

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Contributing Institute(s):

1. Translational Protein Biochemistry (AG Böckers)
2. Clinical Study Center (Ulm) (Clinical Study Center (Ulm))
3. Translational Mass Spectrometry and Biomarker Research (AG Öckl)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)
2. 353 - Clinical and Health Care Research (POF4-353) (POF4-353)

Appears in the scientific report 2026

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Linked articles:

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Journal Article Brenner, D. (First author)DZNE* ; Ponomarenko, A. ; Petrut, I. ; Beyrle, S. ; Contardo, M. ; Loss, I. ; Radke, C. ; Frank, J. ; Zimmer, E. ; Schlesner, M. ; Achenbach, P. ; Scheveneels, W. ; Aly, A. ; Nazlican, H. ; Hesebeck-Brinkmann, J. ; Oeckl, P.DZNE* ; Müller, K. ; Siebert, R. ; Böckers, T.DZNE* ; van Eijk, K. ; Veldink, J. ; Kleger, A. ; Mulaw, M. ; Andersen, P. M. ; Forsberg, K. ; Weishaupt, J. H.DZNE* ; Loghmani, S. B. ; Grehl, T. ; van Damme, P. ; Weis, J. ; Catanese, A. (Last author)DZNE*
A rare missense variant impacting NEK1 kinase function is associated with ALS.
Acta Neuropathologica Communications 14(1), 135 (2026) [10.1186/s40478-026-02351-6]2026   Files  Fulltext by Pubmed Central BibTeX | EndNote: XML, Text | RIS

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